7DDQ image
Deposition Date 2020-10-29
Release Date 2021-06-30
Last Version Date 2026-08-12
Entry Detail
PDB ID:
7DDQ
Keywords:
PHOTOSYNTHESIS
Title:
Structure of RC-LH1-PufX from Rhodobacter veldkampii
Biological Source:
Source Organism(s):
Rhodobacter veldkampii DSM 11550 (Taxon ID: 1185920)
Method Details:
Experimental Method:
ELECTRON MICROSCOPY
Resolution:
2.84 Å
Aggregation State:
PARTICLE
Reconstruction Method:
SINGLE PARTICLE
7DDQ validation report missing
Macromolecular Entities
Structures with similar UniProt ID
Structural Superimposition Protein Blast
Polymer Type:polypeptide(L)
Molecule:Photosynthetic reaction cente
Gene (Uniprot):puhA
Chain IDs:DA (auth: H)
Chain Length:252
Number of Molecules:1
Biological Source:Rhodobacter veldkampii DSM 11550
UniProt ID:A0A2T4JIP4 Pfam ID:PF03967, PF05239
Structures with similar UniProt ID
Structural Superimposition Protein Blast
Polymer Type:polypeptide(L)
Molecule:Photosynthetic reaction cente
Gene (Uniprot):C5F46_07915
Chain IDs:BA (auth: L)
Chain Length:276
Number of Molecules:1
Biological Source:Rhodobacter veldkampii DSM 11550
UniProt ID:A0A2T4JIS6 Pfam ID:PF00124
Structures with similar UniProt ID
Structural Superimposition Protein Blast
Polymer Type:polypeptide(L)
Molecule:Reaction center protein M cha
Gene (Uniprot):C5F46_07920
Chain IDs:CA (auth: M)
Chain Length:308
Number of Molecules:1
Biological Source:Rhodobacter veldkampii DSM 11550
UniProt ID:A0A2T4JIN0 Pfam ID:PF00124
Structures with similar UniProt ID
Structural Superimposition Protein Blast
Polymer Type:polypeptide(L)
Molecule:Antenna pigment protein beta
Gene (Uniprot):C5F46_07905
Chain IDs:B (auth: N), D (auth: S), F (auth: O), H (auth: U), J (auth: D), L (auth: A), N (auth: J), P (auth: E), R (auth: T), U (auth: R), W (auth: K), Y (auth: G), AA (auth: I), FA (auth: F), HA (auth: B)
Chain Length:48
Number of Molecules:15
Biological Source:Rhodobacter veldkampii DSM 11550
UniProt ID:A0A2T4JIL7 Pfam ID:PF00556
Structures with similar UniProt ID
Structural Superimposition Protein Blast
Polymer Type:polypeptide(L)
Molecule:PufX
Gene (Uniprot):C5F46_07925
Chain IDs:S (auth: X)
Chain Length:83
Number of Molecules:1
Biological Source:Rhodobacter veldkampii DSM 11550
UniProt ID:A0A2T4JIP3 Pfam ID:PF11511
Structures with similar UniProt ID
Structural Superimposition Protein Blast
Polymer Type:polypeptide(L)
Molecule:Antenna pigment protein alpha
Gene (Uniprot):C5F46_07910
Chain IDs:A (auth: o), C (auth: t), E (auth: r), G (auth: a), I (auth: e), K (auth: b), M (auth: k), O (auth: f), Q (auth: u), T (auth: s), V (auth: n), X (auth: i), Z (auth: j), EA (auth: g), GA (auth: d)
Chain Length:57
Number of Molecules:15
Biological Source:Rhodobacter veldkampii DSM 11550
UniProt ID:A0A2T4JIR4 Pfam ID:PF00556
Ligand Molecules
3PE
BCL
BPH
FE
SPO
U10
Primary Citation
Cryo-EM structure of the photosynthetic RC-LH1-PufX supercomplex at 2.8-angstrom resolution.
Sci Adv 7 ? ? (2021)
PMID: 34134992 DOI: 10.1126/sciadv.abf8864

Abstact

The reaction center (RC)-light-harvesting complex 1 (LH1) supercomplex plays a pivotal role in bacterial photosynthesis. Many RC-LH1 complexes integrate an additional protein PufX that is key for bacterial growth and photosynthetic competence. Here, we present a cryo-electron microscopy structure of the RC-LH1-PufX supercomplex from Rhodobacter veldkampii at 2.8-Å resolution. The RC-LH1-PufX monomer contains an LH ring of 15 αβ-polypeptides with a 30-Å gap formed by PufX. PufX acts as a molecular "cross brace" to reinforce the RC-LH1 structure. The unusual PufX-mediated large opening in the LH1 ring and defined arrangement of proteins and cofactors provide the molecular basis for the assembly of a robust RC-LH1-PufX supercomplex and efficient quinone transport and electron transfer. These architectural features represent the natural strategies for anoxygenic photosynthesis and environmental adaptation.

Legend

Protein

Chemical

Disease

Primary Citation of related structures
7DDQ
Feedback Form
Name
Email
Institute
Feedback