1j54
From Proteopedia
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Structure of the N-terminal exonuclease domain of the epsilon subunit of E.coli DNA polymerase III at pH 5.8
Overview
The epsilon subunit of the Escherichia coli replicative DNA polymerase III, is the proofreading 3'-5' exonuclease. Structures of its catalytic, N-terminal domain (epsilon186) were determined at two pH values (5.8 and, 8.5) at resolutions of 1.7-1.8 A, in complex with two Mn(II) ions and a, nucleotide product of its reaction, thymidine 5'-monophosphate. The, protein structure is built around a core five-stranded beta sheet that is, a common feature of members of the DnaQ superfamily. The structures were, identical, except for differences in the way TMP and water molecules are, coordinated to the binuclear metal center in the active site. These data, are used to develop a mechanism for epsilon and to produce a plausible, model of the complex of epsilon186 with DNA.
About this Structure
1J54 is a Single protein structure of sequence from Escherichia coli with MN, TMP and EDO as ligands. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 Full crystallographic information is available from OCA.
Reference
Structural basis for proofreading during replication of the Escherichia coli chromosome., Hamdan S, Carr PD, Brown SE, Ollis DL, Dixon NE, Structure. 2002 Apr;10(4):535-46. PMID:11937058
Page seeded by OCA on Tue Nov 20 17:56:37 2007
