1egr

SEQUENCE-SPECIFIC 1H N.M.R. ASSIGNMENTS AND DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF REDUCED ESCHERICHIA COLI GLUTAREDOXINSEQUENCE-SPECIFIC 1H N.M.R. ASSIGNMENTS AND DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF REDUCED ESCHERICHIA COLI GLUTAREDOXIN

Structural highlights 1egr is a 1 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GLRX1_ECOLI The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfide bonds in a coupled system with glutathione reductase. 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 determination of the nuclear magnetic resonance structure of reduced E. coli glutaredoxin in aqueous solution is described. Based on nearly complete, sequence-specific resonance assignments, 813 nuclear Overhauser effect distance constraints and 191 dihedral angle constraints were employed as the input for the structure calculations, for which the distance geometry program DIANA was used followed by simulated annealing with the program X-PLOR. The molecular architecture of reduced glutaredoxin is made up of three helices and four-stranded beta-sheet. The first strand of the beta-sheet (residues 2 to 7) runs parallel to the second strand (32 to 37) and antiparallel to the third strand (61 to 64), and the sheet is extended in an antiparallel fashion with a fourth strand (67 to 69). The first helix with residues 13 to 28 and the last helix (71 to 83) run parallel to each other on one side of the beta-sheet, with their direction opposite to that of the two parallel beta-strands, and the helix formed by residues 44 to 53 fills space available due to the twist of the beta-sheet and the reduced length of the last two beta-strands. The active site Cys11-Pro-Tyr-Cys14 is located after the first beta-strand and occupies the latter part of the loop connecting this strand with the first helix. Sequence-specific 1H n.m.r. assignments and determination of the three-dimensional structure of reduced Escherichia coli glutaredoxin.,Sodano P, Xia TH, Bushweller JH, Bjornberg O, Holmgren A, Billeter M, Wuthrich K J Mol Biol. 1991 Oct 20;221(4):1311-24. PMID:1942053 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 1egr Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image