1hk8

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File:1hk8.gif


1hk8, resolution 2.45Å

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STRUCTURAL BASIS FOR ALLOSTERIC SUBSTRATE SPECIFICITY REGULATION IN CLASS III RIBONUCLEOTIDE REDUCTASES: NRDD IN COMPLEX WITH DGTP

OverviewOverview

A Zn(Cys)(4) center has been found in the C-terminal region of the crystal, structure of the anaerobic class III ribonucleotide reductase (RNR) from, bacteriophage T4. The metal center is structurally related to the zinc, ribbon motif and to rubredoxin and rubrerythrin. Mutant enzymes of the, homologous RNR from Escherichia coli, in which the coordinating cysteines, conserved in almost all known class III RNR sequences, have been mutated, into alanines, are shown to be inactive as the result of their inability, to generate the catalytically essential glycyl radical. The possible roles, of the metal center are discussed in relationship to the currently, proposed reaction mechanism for generation of the glycyl radical in class, III RNRs.

About this StructureAbout this Structure

1HK8 is a Single protein structure of sequence from Enterobacteria phage t2 with ZN, MN and DGT as ligands. This structure superseeds the now removed PDB entry 1H77. Active as Ribonucleoside-triphosphate reductase, with EC number 1.17.4.2 Structure known Active Site: DG1. Full crystallographic information is available from OCA.

ReferenceReference

A metal-binding site in the catalytic subunit of anaerobic ribonucleotide reductase., Logan DT, Mulliez E, Larsson KM, Bodevin S, Atta M, Garnaud PE, Sjoberg BM, Fontecave M, Proc Natl Acad Sci U S A. 2003 Apr 1;100(7):3826-31. Epub 2003 Mar 24. PMID:12655046

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