1HK8

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

Replaces:  1H77

Summary for 1HK8

• Entry DOI: 10.2210/pdb1hk8/pdb
• Related: 1H78 1H79 1H7A 1H7B
• Descriptor: ANAEROBIC RIBONUCLEOTIDE-TRIPHOSPHATE REDUCTASE, 2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE, ZINC ION, ... (5 entities in total)
• Functional Keywords: oxidoreductase, reductase, allosteric regulation, substrate specificity
• Biological source: BACTERIOPHAGE T4
• Total number of polymer chains: 1
• Total formula weight: 69190.30

Authors

Larsson, K.-M.,Andersson, J.,Sjoeberg, B.-M.,Nordlund, P.,Logan, D.T. (deposition date: 2003-03-06, release date: 2003-03-27, Last modification date: 2023-12-13)

Primary citation

Logan, D.T.,Mulliez, E.,Larsson, K.-M.,Bodevin, S.,Atta, M.,Garnaud, P.E.,Sjoberg, B.-M.,Fontecave, M.
A Metal-Binding Site in the Catalytic Subunit of Anaerobic Ribonucleotide Reductase.
Proc.Natl.Acad.Sci.USA, 100:3826-, 2003

PubMed Abstract: 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.

PubMed: 12655046
DOI: 10.1073/PNAS.0736456100

Experimental method

X-RAY DIFFRACTION (2.45 Å)