9Q87 image
Deposition Date 2025-02-23
Release Date 2025-05-14
Last Version Date 2026-04-01
Entry Detail
PDB ID:
9Q87
Keywords:
Title:
Principles of ion binding to RNA inferred from the analysis of a 1.55 Angstrom resolution bacterial ribosome structure - Part I: Mg2+
Biological Source:
Source Organism(s):
Method Details:
Experimental Method:
Resolution:
1.55 Å
Aggregation State:
PARTICLE
Reconstruction Method:
SINGLE PARTICLE
Macromolecular Entities
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Large ribosomal subunit prote
Gene (Uniprot):rpmG
Chain IDs:X (auth: 0)
Chain Length:55
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Large ribosomal subunit prote
Gene (Uniprot):rpmH
Chain IDs:Y (auth: 1)
Chain Length:46
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Large ribosomal subunit prote
Gene (Uniprot):rpmI
Chain IDs:Z (auth: 2)
Chain Length:65
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Large ribosomal subunit prote
Gene (Uniprot):rpmJ
Chain IDs:AA (auth: 3)
Chain Length:38
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Large ribosomal subunit prote
Gene (Uniprot):rplK
Chain IDs:BA (auth: 5)
Chain Length:141
Number of Molecules:1
Biological Source:Escherichia coli B
Polymer Type:polyribonucleotide
Molecule:A-site tRNA
Chain IDs:CA (auth: 6)
Chain Length:2
Number of Molecules:1
Biological Source:Escherichia coli B
Polymer Type:polyribonucleotide
Molecule:30S
Chain IDs:A
Chain Length:2908
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Small ribosomal subunit prote
Gene (Uniprot):rpsB
Chain IDs:B
Chain Length:233
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Small ribosomal subunit prote
Gene (Uniprot):rpsC
Chain IDs:C
Chain Length:273
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Small ribosomal subunit prote
Gene (Uniprot):rpsD
Chain IDs:D
Chain Length:206
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Small ribosomal subunit prote
Gene (Uniprot):rpsE
Chain IDs:E
Chain Length:201
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Small ribosomal subunit prote
Gene (Uniprot):rpsF
Chain IDs:F
Chain Length:135
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Small ribosomal subunit prote
Gene (Uniprot):rpsG
Chain IDs:G
Chain Length:177
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Small ribosomal subunit prote
Gene (Uniprot):rpsH
Chain IDs:H
Chain Length:130
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Small ribosomal subunit prote
Gene (Uniprot):rpsI
Chain IDs:I
Chain Length:130
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Small ribosomal subunit prote
Gene (Uniprot):rpsJ
Chain IDs:J
Chain Length:103
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Small ribosomal subunit prote
Gene (Uniprot):rpsK
Chain IDs:K
Chain Length:144
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Small ribosomal subunit prote
Gene (Uniprot):rpsL
Chain IDs:L
Chain Length:124
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Small ribosomal subunit prote
Gene (Uniprot):rpsM
Chain IDs:M
Chain Length:127
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Small ribosomal subunit prote
Gene (Uniprot):rpsN
Chain IDs:N
Chain Length:101
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Small ribosomal subunit prote
Gene (Uniprot):rpsO
Chain IDs:O
Chain Length:89
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Small ribosomal subunit prote
Gene (Uniprot):rpsP
Chain IDs:P
Chain Length:118
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Small ribosomal subunit prote
Gene (Uniprot):rpsQ
Chain IDs:Q
Chain Length:84
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Small ribosomal subunit prote
Gene (Uniprot):rpsR
Chain IDs:R
Chain Length:75
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Small ribosomal subunit prote
Gene (Uniprot):rpsS
Chain IDs:S
Chain Length:92
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Small ribosomal subunit prote
Gene (Uniprot):rpsT
Chain IDs:T
Chain Length:87
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Small ribosomal subunit prote
Gene (Uniprot):rpsU
Chain IDs:U
Chain Length:94
Number of Molecules:1
Biological Source:Escherichia coli B
Polymer Type:polyribonucleotide
Molecule:mRNA
Chain IDs:V (auth: X)
Chain Length:6
Number of Molecules:1
Biological Source:Escherichia coli B
Polymer Type:polyribonucleotide
Molecule:P-site tRNA
Chain IDs:W (auth: Z)
Chain Length:77
Number of Molecules:1
Biological Source:Escherichia coli B
Polymer Type:polyribonucleotide
Molecule:23S rRNA
Chain IDs:DA (auth: a)
Chain Length:2908
Number of Molecules:1
Biological Source:Escherichia coli B
Polymer Type:polyribonucleotide
Molecule:5S rRNA
Chain IDs:EA (auth: b)
Chain Length:233
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Large ribosomal subunit prote
Gene (Uniprot):rplB
Chain IDs:FA (auth: c)
Chain Length:273
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Large ribosomal subunit prote
Gene (Uniprot):rplC
Chain IDs:GA (auth: d)
Chain Length:206
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Large ribosomal subunit prote
Gene (Uniprot):rplD
Chain IDs:HA (auth: e)
Chain Length:201
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Large ribosomal subunit prote
Gene (Uniprot):rplE
Chain IDs:IA (auth: f)
Chain Length:135
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Large ribosomal subunit prote
Gene (Uniprot):rplF
Chain IDs:JA (auth: g)
Chain Length:177
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Large ribosomal subunit prote
Gene (Uniprot):rplI
Chain IDs:KA (auth: h)
Chain Length:130
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Large ribosomal subunit prote
Gene (Uniprot):rplM
Chain IDs:LA (auth: i)
Chain Length:130
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Large ribosomal subunit prote
Gene (Uniprot):rplN
Chain IDs:MA (auth: j)
Chain Length:103
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Large ribosomal subunit prote
Gene (Uniprot):rplO
Chain IDs:NA (auth: k)
Chain Length:144
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Large ribosomal subunit prote
Chain IDs:OA (auth: l)
Chain Length:124
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Large ribosomal subunit prote
Gene (Uniprot):rplQ
Chain IDs:PA (auth: m)
Chain Length:127
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Large ribosomal subunit prote
Gene (Uniprot):rplR
Chain IDs:QA (auth: n)
Chain Length:101
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Large ribosomal subunit prote
Gene (Uniprot):rplS
Chain IDs:RA (auth: o)
Chain Length:89
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Large ribosomal subunit prote
Gene (Uniprot):rplT
Chain IDs:SA (auth: p)
Chain Length:118
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Large ribosomal subunit prote
Gene (Uniprot):rplU
Chain IDs:TA (auth: q)
Chain Length:84
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Large ribosomal subunit prote
Gene (Uniprot):rplV
Chain IDs:UA (auth: r)
Chain Length:75
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Large ribosomal subunit prote
Gene (Uniprot):rplW
Chain IDs:VA (auth: s)
Chain Length:92
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Large ribosomal subunit prote
Gene (Uniprot):rplX
Chain IDs:WA (auth: t)
Chain Length:87
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Large ribosomal subunit prote
Gene (Uniprot):rplY
Chain IDs:XA (auth: u)
Chain Length:94
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Large ribosomal subunit prote
Gene (Uniprot):rpmA
Chain IDs:YA (auth: v)
Chain Length:85
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Large ribosomal subunit prote
Gene (Uniprot):rpmB
Chain IDs:ZA (auth: w)
Chain Length:78
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Large ribosomal subunit prote
Gene (Uniprot):rpmC
Chain IDs:AB (auth: x)
Chain Length:6
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Large ribosomal subunit prote
Gene (Uniprot):rpmD
Chain IDs:BB (auth: y)
Chain Length:59
Number of Molecules:1
Biological Source:Escherichia coli B
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Large ribosomal subunit prote
Gene (Uniprot):rpmF
Chain IDs:CB (auth: z)
Chain Length:77
Number of Molecules:1
Biological Source:Escherichia coli B
Modified Residue
Compound ID Chain ID Parent Comp ID Details 2D Image
2MG A G modified residue
4D4 OA ARG modified residue
4OC A C modified residue
4SU W U modified residue
5MC A C modified residue
5MU W U modified residue
D2T L ASP modified residue
G7M A G modified residue
H2U W U modified residue
MA6 A A modified residue
MEQ GA GLN modified residue
OMC W C modified residue
PSU A U modified residue
UR3 A U modified residue
Primary Citation
Principles of ion binding to RNA inferred from the analysis of a 1.55 angstrom resolution bacterial ribosome structure - Part I: Mg2.
Nucleic Acids Res. 53 ? ? (2025)
PMID: 39791453 DOI: 10.1093/nar/gkae1148

Abstact

The importance of Mg2+ ions for RNA structure and function cannot be overstated. Several attempts were made to establish a comprehensive Mg2+ binding site classification. However, such descriptions were hampered by poorly modelled ion binding sites as observed in a recent cryo-EM 1.55 Å Escherichia coli ribosome structure where incomplete ion assignments blurred our understanding of their binding patterns. We revisited this model to establish general binding principles applicable to any RNA of sufficient resolution. These principles rely on the 2.9 Å distance separating two water molecules bound in cis to Mg2+. By applying these rules, we could assign all Mg2+ ions bound with 2-4 non-water oxygens. We also uncovered unanticipated motifs where up to five adjacent nucleotides wrap around a single ion. The formation of such motifs involves a hierarchical Mg2+ ion dehydration process that plays a significant role in ribosome biogenesis and in the folding of large RNAs. Besides, we established a classification of the Mg2+…Mg2+ and Mg2+…K+ ion pairs observed in this ribosome. Overall, the uncovered binding principles enhance our understanding of the roles of ions in RNA structure and will help refining the solvation shell of other RNA systems.

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