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Cryo-EM structure of the rhodospirillum rubrum rc-LH1 complex

Analyse Cryo-EM structure of the rhodospirillum rubrum rc-LH1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7OY8
Type
protein
Length
2,293 residues
Chains
35
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Light-harvesting protein B-870 beta chain; Antenna complex, ALPHA/BETA subunit…
UniProt
Q2RQ23, Q2RQ24, Q2RWS4, Q2RQ25, Q2RQ26
Ligands
07D, CRT, U10, PGW, CD4, BPH, RQ0, FE, CL, PO4
Pockets
20 · best druggability 0.81

Structure

electron microscopy · 12 distinct chains · 57% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
1, 3, 5, 7, I, O, U, W, d, nLight-harvesting protein B-870 beta chainprotein4473% helix, 5% strandQ2RQ23
2, A, E, J, N, VAntenna complex, ALPHA/BETA subunitprotein4663% helix, 0% strandQ2RQ24
4, 6, D, F, G, T, X, ZAntenna complex, ALPHA/BETA subunitprotein4762% helix, 0% strandQ2RQ24
8Antenna complex, ALPHA/BETA subunitprotein4856% helix, 0% strandQ2RQ24
9Light-harvesting protein B-870 beta chainprotein4670% helix, 4% strandQ2RQ23
HPhotosynthetic reaction center, H-chainprotein25726% helix, 24% strandQ2RWS4
K, S, mLight-harvesting protein B-870 beta chainprotein4571% helix, 4% strandQ2RQ23
LPhotosynthetic reaction center L subunitprotein27466% helix, 4% strandQ2RQ25
MReaction center protein M chainprotein30564% helix, 5% strandQ2RQ26
QLight-harvesting protein B-870 beta chainprotein4768% helix, 4% strandQ2RQ23
RAntenna complex, ALPHA/BETA subunitprotein4663% helix, 0% strandQ2RQ24
YLight-harvesting protein B-870 beta chainprotein4374% helix, 5% strandQ2RQ23

Ligands and binding sites

  • 07D · Trans-Geranyl BACTERIOCHLOROPHYLL A · ligand · 37 copies · chains 1, X, Z, n, 2, 3, 4, 5, 6, M, 7, 8, 9, D, A, R, W, E, I, F, K, G, H, O, Q, J, N, S, U, L, T, Y, V, d, m
  • CRT · Spirilloxanthin · ligand · 17 copies · chains 1, 2, X, Z, 3, 4, 5, 6, 7, 8, 9, D, E, I, A, J, N, U, F, K, M, R, W, G, O, Q, S, T, Y, V, d, m, n
  • U10 · Ubiquinone-10 · ligand · 3 copies · chains L, M, A, N, R, J
  • PGW · (1R)-2-{[(S)-{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy) phosphoryl]oxy}-1-[(hexadecanoyloxy)methyl]ethyl (9Z)-octadec-9-enoate · ligand · 2 copies · chains H, L, M, G, J
  • CD4 · (2R,5R,11R,14R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-2,14-bis(tetradecanoyloxy)-4,6,10,12,16-pentaoxa-5,11-diphosphatriacont-1-yl tetradecanoate · ligand · 2 copies · chains H, J, L, M, D, E
  • BPH · Bacteriopheophytin A · ligand · 2 copies · chains L, M, 4
  • RQ0 · 2-azanyl-5-[(2~{E},6~{E},8~{E},10~{E},12~{E},14~{E}, 18~{E},22~{E},26~{E},30~{E},34~{E})-3,7,11,15,19,23, 27,31,35,39-decamethyltetraconta-2,6,8,10,12,14,18,22, 26,30,34,38-dodecaenyl]-3-methoxy-6-methyl-cyclohexa-2,5-diene-1,4-dione · ligand · chains L, M
  • FE · Fe (III) ion · metal · chains L, M
  • CL · Chloride ion · ion · chains H, M
  • PO4 · Phosphate ion · ion · chains 8, M
  • LMT · Dodecyl-beta-D-maltoside · additive · chains L, R, T

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
112000.810.8296BPH, 07D
21950.800.9544empty
38270.800.8281CRT, PO4
49810.770.7976U10
511900.750.78105CRT

Interfaces

98 interfaces between chains.

  • L–M · 4472 Ų buried · 58 hydrogen bonds · protein-protein
  • H–M · 2901 Ų buried · 44 hydrogen bonds · protein-protein
  • H–L · 1578 Ų buried · 22 hydrogen bonds · protein-protein
  • G–Q · 837 Ų buried · 10 hydrogen bonds · protein-protein
  • 6–M · 797 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 15 modified (formylation).

Compared structures

  • 7OY8 · Cryo-EM structure of the Rhodospirillum rubrum RC-LH1 complex · the same entry in another collection · chain A against A, TM-score 1.00

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