5IYC image
Deposition Date 2016-03-24
Release Date 2016-05-18
Last Version Date 2024-03-06
Entry Detail
PDB ID:
5IYC
Title:
Human core-PIC in the initial transcribing state
Biological Source:
Source Organism(s):
Homo sapiens (Taxon ID: 9606)
Expression System(s):
Method Details:
Experimental Method:
Resolution:
3.90 Å
Aggregation State:
PARTICLE
Reconstruction Method:
SINGLE PARTICLE
Macromolecular Entities
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerase I
Gene (Uniprot):POLR2A
Chain IDs:A
Chain Length:1970
Number of Molecules:1
Biological Source:Homo sapiens
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerase I
Gene (Uniprot):POLR2B
Chain IDs:B
Chain Length:1174
Number of Molecules:1
Biological Source:Homo sapiens
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerase I
Gene (Uniprot):POLR2C
Chain IDs:C
Chain Length:275
Number of Molecules:1
Biological Source:Homo sapiens
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerase I
Gene (Uniprot):POLR2D
Chain IDs:D
Chain Length:142
Number of Molecules:1
Biological Source:Homo sapiens
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerase I
Gene (Uniprot):POLR2E
Chain IDs:E
Chain Length:210
Number of Molecules:1
Biological Source:Homo sapiens
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerase I
Gene (Uniprot):POLR2F
Chain IDs:F
Chain Length:127
Number of Molecules:1
Biological Source:Homo sapiens
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerase I
Gene (Uniprot):POLR2G
Chain IDs:G
Chain Length:172
Number of Molecules:1
Biological Source:Homo sapiens
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerase I
Gene (Uniprot):POLR2H
Chain IDs:H
Chain Length:150
Number of Molecules:1
Biological Source:Homo sapiens
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerase I
Gene (Uniprot):POLR2I
Chain IDs:I
Chain Length:125
Number of Molecules:1
Biological Source:Homo sapiens
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerase I
Gene (Uniprot):POLR2L
Chain IDs:J
Chain Length:67
Number of Molecules:1
Biological Source:Homo sapiens
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerase I
Gene (Uniprot):POLR2J
Chain IDs:K
Chain Length:117
Number of Molecules:1
Biological Source:Homo sapiens
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerase I
Gene (Uniprot):POLR2K
Chain IDs:L
Chain Length:58
Number of Molecules:1
Biological Source:Homo sapiens
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Transcription initiation fact
Gene (Uniprot):GTF2B
Chain IDs:M
Chain Length:316
Number of Molecules:1
Biological Source:Homo sapiens
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Transcription initiation fact
Gene (Uniprot):GTF2A1
Chain IDs:N
Chain Length:376
Number of Molecules:1
Biological Source:Homo sapiens
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Transcription initiation fact
Gene (Uniprot):GTF2A2
Chain IDs:O
Chain Length:109
Number of Molecules:1
Biological Source:Homo sapiens
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:TATA-box-binding protein
Gene (Uniprot):TBP
Chain IDs:P
Chain Length:339
Number of Molecules:1
Biological Source:Homo sapiens
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:General transcription factor
Gene (Uniprot):GTF2E1
Chain IDs:Q
Chain Length:439
Number of Molecules:1
Biological Source:Homo sapiens
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Transcription initiation fact
Gene (Uniprot):GTF2E2
Chain IDs:R
Chain Length:291
Number of Molecules:1
Biological Source:Homo sapiens
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:General transcription factor
Gene (Uniprot):GTF2F1
Chain IDs:S
Chain Length:517
Number of Molecules:1
Biological Source:Homo sapiens
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:General transcription factor
Gene (Uniprot):GTF2F2
Chain IDs:T
Chain Length:249
Number of Molecules:1
Biological Source:Homo sapiens
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Transcription elongation fact
Gene (Uniprot):TCEA1
Chain IDs:U
Chain Length:301
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polydeoxyribonucleotide
Molecule:SCP-X
Chain IDs:V (auth: X)
Chain Length:80
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polydeoxyribonucleotide
Molecule:SCP-Y
Chain IDs:W (auth: Y)
Chain Length:80
Number of Molecules:1
Biological Source:Homo sapiens
Primary Citation
Near-atomic resolution visualization of human transcription promoter opening.
Nature 533 359 365 (2016)
PMID: 27193682 DOI: 10.1038/nature17970

Abstact

In eukaryotic transcription initiation, a large multi-subunit pre-initiation complex (PIC) that assembles at the core promoter is required for the opening of the duplex DNA and identification of the start site for transcription by RNA polymerase II. Here we use cryo-electron microscropy (cryo-EM) to determine near-atomic resolution structures of the human PIC in a closed state (engaged with duplex DNA), an open state (engaged with a transcription bubble), and an initially transcribing complex (containing six base pairs of DNA-RNA hybrid). Our studies provide structures for previously uncharacterized components of the PIC, such as TFIIE and TFIIH, and segments of TFIIA, TFIIB and TFIIF. Comparison of the different structures reveals the sequential conformational changes that accompany the transition from each state to the next throughout the transcription initiation process. This analysis illustrates the key role of TFIIB in transcription bubble stabilization and provides strong structural support for a translocase activity of XPB.

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