| Structural highlights
1e6d is a 3 chain structure with sequence from "rhodococcus_capsulatus"_molisch_1907 "rhodococcus capsulatus" molisch 1907. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , , , , |
| Related: | 1qov, 1mps, 1e14, 1dv3, 1dv6, 1ds8, 1aij, 1aig, 2rcr, 4rcr, 1pss, 1pst, 1pcr, 1yst |
| Gene: | PUFQLMX ("Rhodococcus capsulatus" Molisch 1907) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum |
Function
[RCEH_RHOSH] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. [RCEM_RHOSH] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. [RCEL_RHOSH] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
A series of reaction centres bearing mutations at the (Phe) M197 position were constructed in the photosynthetic bacterium Rhodobacter sphaeroides. This residue is adjacent to the pair of bacteriochlorophyll molecules (P(L) and P(M)) that is the primary donor of electrons (P) in photosynthetic light-energy transduction. All of the mutations affected the optical and electrochemical properties of the P bacteriochlorophylls. A mutant reaction centre with the change Phe M197 to Arg (FM197R) was crystallized, and a structural model constructed at 2.3 A (1 A=0.1 nm) resolution. The mutation resulted in a change in the structure of the protein at the interface region between the P bacteriochlorophylls and the monomeric bacteriochlorophyll that is the first electron acceptor (B(L)). The new Arg residue at the M197 position undergoes a significant reorientation, creating a cavity at the interface region between P and B(L). The acetyl carbonyl substituent group of the P(M) bacteriochlorophyll undergoes an out-of-plane rotation, which decreases the edge-to-edge distance between the macrocycles of P(M) and B(L). In addition, two new buried water molecules partially filled the cavity that is created by the reorientation of the Arg residue. These waters are in a suitable position to connect the macrocycles of P and B(L) via three hydrogen bonds. Transient absorption measurements show that, despite an inferred decrease in the driving force for primary electron transfer in the FM197R reaction centre, there is little effect on the overall rate of the primary reaction in the bulk of the reaction-centre population. Examination of the X-ray crystal structure reveals a number of small changes in the structure of the reaction centre in the interface region between the P and B(L) bacteriochlorophylls that could account for this faster-than-predicted rate of primary electron transfer.
An examination of how structural changes can affect the rate of electron transfer in a mutated bacterial photoreaction centre.,Ridge JP, Fyfe PK, McAuley KE, van Brederode ME, Robert B, van Grondelle R, Isaacs NW, Cogdell RJ, Jones MR Biochem J. 2000 Nov 1;351 Pt 3:567-78. PMID:11042110[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ridge JP, Fyfe PK, McAuley KE, van Brederode ME, Robert B, van Grondelle R, Isaacs NW, Cogdell RJ, Jones MR. An examination of how structural changes can affect the rate of electron transfer in a mutated bacterial photoreaction centre. Biochem J. 2000 Nov 1;351 Pt 3:567-78. PMID:11042110
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