2boz

Photosynthetic Reaction Center Mutant With Gly M203 Replaced With Leu

spinqualitylabelsall models 2boz, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2boz 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, D10, FE, LDA, PO4, SPN, U10 Related: 1aig, 1aij, 1ds8, 1dv3, 1dv6, 1e14, 1e6d, 1f6n, 1fnp, 1fnq, 1jgw, 1jgx, 1jgy, 1jgz, 1jh0, 1k6l, 1k6n, 1kby, 1l9b, 1l9j, 1m3x, 1mps, 1ogv, 1pcr, 1pss, 1pst, 1qov, 1rg5, 1rgn, 1rqk, 1rvj, 1ry5, 1rzh, 1rzz, 1s00, 1umx, 1yst, 2bfj, 2bfs, 2bft, 2bnp, 2bns, 2rcr, 4rcr 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 The role of a water molecule (water A) located between the primary electron donor (P) and first electron acceptor bacteriochlorophyll (B(A)) in the purple bacterial reaction center was investigated by mutation of glycine M203 to leucine (GM203L). The x-ray crystal structure of the GM203L reaction center shows that the new leucine residue packs in such a way that water A is sterically excluded from the complex, but the structure of the protein-cofactor system around the mutation site is largely undisturbed. The results of absorbance and resonance Raman spectroscopy were consistent with either the removal of a hydrogen bond interaction between water A and the keto carbonyl group of B(A) or a change in the local electrostatic environment of this carbonyl group. Similarities in the spectroscopic properties and x-ray crystal structures of reaction centers with leucine and aspartic acid mutations at the M203 position suggested that the effects of a glycine to aspartic acid substitution at the M203 position can also be explained by steric exclusion of water A. In the GM203L mutant, loss of water A was accompanied by an approximately 8-fold slowing of the rate of decay of the primary donor excited state, indicating that the presence of water A is important for optimization of the rate of primary electron transfer. Possible functions of this water molecule are discussed, including a switching role in which the redox potential of the B(A) acceptor is rapidly modulated in response to oxidation of the primary electron donor. Strong effects of an individual water molecule on the rate of light-driven charge separation in the Rhodobacter sphaeroides reaction center.,Potter JA, Fyfe PK, Frolov D, Wakeham MC, van Grondelle R, Robert B, Jones MR J Biol Chem. 2005 Jul 22;280(29):27155-64. Epub 2005 May 20. PMID:15908429 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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