1e14 | pdb_00001e14

PHOTOSYNTHETIC REACTION CENTER MUTANT WITH PHE M197 REPLACED WITH ARG (CHAIN M, FM197R) AND GLY M203 REPLACED WITH ASP (CHAIN M, GM203D)

spinqualitylabelsall models 1e14, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1e14 is a 3 chain structure with sequence from Rhodobacter sphaeroides. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BCL, BPH, CDL, FE, LDA, SPN, U10 Related: 1qov, 2rcr, 4rcr, 1pss, 1pst, 1pcr, 1aig, 1aij, 1yst, 1mps Gene: PUFQLMX (Rhodobacter sphaeroides) Resources: FirstGlance, OCA, RCSB, PDBsum 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 Reaction centers with the double mutation Phe M197 to Arg and Gly M203 to Asp (FM197R/GM203D) have been crystallized from an antenna-deficient strain of Rhodobacter sphaeroides, and the structure has been determined at 2.7 A resolution. Unlike in reaction centers with a single FM197R mutation, the Arg M197 residue in the FM197R/GM203D reaction center adopts a position similar to that of the native Phe residue in the wild-type reaction center. Asp M203 is packed in such a way that the gamma-carboxy group interacts with the backbone carbonyl of Arg M197. The Asp M203 residue takes up part of the volume that is occupied in the wild-type reaction center by a water molecule. This water has been proposed to form a hydrogen bond interaction with the 9-keto carbonyl group of the active branch accessory bacteriochlorophyll, particularly when the primary donor bacteriochlorophylls are oxidized. The GM203D mutation therefore appears to remove the possibility of this hydrogen bond interaction by exclusion of this water molecule, as well as altering the local dielectric environment of the 9-keto carbonyl group. We examine whether the observed structural changes can provide new or alternative explanations for the absorbance and electron-transfer properties of reaction centers with the FM197R and GM203D mutations. Structural consequences of the replacement of glycine M203 with aspartic acid in the reaction center from Rhodobacter sphaeroides.,Fyfe PK, Ridge JP, McAuley KE, Cogdell RJ, Isaacs NW, Jones MR Biochemistry. 2000 May 23;39(20):5953-60. PMID:10821666 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA