1kgo | pdb_00001kgo

R2F from Corynebacterium Ammoniagenes in its reduced, Fe containing, form

spinqualitylabelsall models 1kgo, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1kgo is a 4 chain structure with sequence from "bacterium_ammoniagenes"_cooke_and_keith_1927 "bacterium ammoniagenes" cooke and keith 1927. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FE2 Related: 1kgn, 1kgp Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [O69274_CORAM] Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity).[PIRNR:PIRNR000355] 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 Ribonucleotide reductase (RNR) is the enzyme performing de novo production of the four deoxyribonucleotides needed for DNA synthesis. All mammals as well as some prokaryotes express the class I enzyme which is an alpha(2)beta(2) protein. The smaller of the homodimers, denoted R2, contains a di-iron carboxylate site which, upon reaction with molecular oxygen, generates a stable tyrosyl radical needed for catalysis. The three-dimensional structure of the oxidized class Ib RNR R2 from Corynebacterium ammoniagenes has been determined at 1.85 A resolution and refined to an R-value of 15.8% (R(free) = 21.3%). In addition, structures of both the reduced iron-containing, and manganese-substituted protein have been solved. The C. ammoniagenes R2 has been proposed to be manganese-dependent. The present structure provides evidence that manganese is not oxidized by the protein, in agreement with recent biochemical data, and that no obvious structural abnormalities are seen in the oxidized and reduced iron-containing forms, giving further support that the protein is indeed an iron-dependent RNR R2. The di-manganese structure also provides an explanation for the magnetic properties of this site. The structure of the oxidized C. ammoniagenes R2 also reveals an additional water molecule bridging the radical and the iron site, which has not previously been seen in any other R2 structure and which might have important mechanistic implications. Crystal structure of the di-iron/radical protein of ribonucleotide reductase from Corynebacterium ammoniagenes.,Hogbom M, Huque Y, Sjoberg BM, Nordlund P Biochemistry. 2002 Jan 29;41(4):1381-9. PMID:11802741 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribonucleotide reductase

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