1rpl

From Proteopedia

Revision as of 23:39, 20 November 2007 by OCA (Talk | contribs)
(diff) ←Older revision | Current revision (diff) | Newer revision→ (diff)
Jump to: navigation, search

1rpl, resolution 2.3Å

Drag the structure with the mouse to rotate

2.3 ANGSTROMS CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF DNA POLYMERASE BETA

Overview

The crystal structure of the catalytic domain of rat DNA polymerase beta, (pol beta) has been determined at 2.3 A resolution and refined to an R, factor of 0.22. The mixed alpha/beta protein has three subdomains arranged, in an overall U shape reminiscent of other polymerase structures. The, folding topology of pol beta, however, is unique. Two divalent metals bind, near three aspartic acid residues implicated in the catalytic activity. In, the presence of Mn2+ and dTTP, interpretable electron density is seen for, two metals and the triphosphate, but not the deoxythymidine moiety. The, principal interaction of the triphosphate moiety is with the bound, divalent metals.

About this Structure

1RPL is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

2.3 A crystal structure of the catalytic domain of DNA polymerase beta., Davies JF 2nd, Almassy RJ, Hostomska Z, Ferre RA, Hostomsky Z, Cell. 1994 Mar 25;76(6):1123-33. PMID:8137427

Page seeded by OCA on Wed Nov 21 01:46:34 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools