1e6d

PHOTOSYNTHETIC REACTION CENTER MUTANT WITH TRP M115 REPLACED WITH PHE (CHAIN M, WM115F) PHE M197 REPLACED WITH ARG (CHAIN M, FM197R)

spinqualitylabelsall models 1e6d, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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: BCL, BPH, FE, LDA, PO4, SPN, U10 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, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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