1oyy
From Proteopedia
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Structure of the RecQ Catalytic Core bound to ATP-gamma-S
Overview
RecQ family helicases catalyze critical genome maintenance reactions in, bacterial and eukaryotic cells, playing key roles in several DNA metabolic, processes. Mutations in recQ genes are linked to genome instability and, human disease. To define the physical basis of RecQ enzyme function, we, have determined a 1.8 A resolution crystal structure of the catalytic core, of Escherichia coli RecQ in its unbound form and a 2.5 A resolution, structure of the core bound to the ATP analog ATPgammaS. The RecQ core, comprises four conserved subdomains; two of these combine to form its, helicase region, while the others form unexpected Zn(2+)-binding and, winged-helix motifs. The structures reveal the molecular basis of missense, mutations that cause Bloom's syndrome, a human RecQ-associated disease., Finally, based on findings from the structures, we propose a mechanism for, RecQ activity that could explain its functional coordination with, topoisomerase III.
About this Structure
1OYY is a Single protein structure of sequence from Escherichia coli with ZN, MN and AGS as ligands. Full crystallographic information is available from OCA.
Reference
High-resolution structure of the E.coli RecQ helicase catalytic core., Bernstein DA, Zittel MC, Keck JL, EMBO J. 2003 Oct 1;22(19):4910-21. PMID:14517231
Page seeded by OCA on Tue Nov 20 23:18:47 2007
Categories: Escherichia coli | Single protein | Bernstein, D.A. | Keck, J.L. | Zittel, M.C. | AGS | MN | ZN | Atp binding | Atp(gamma)s | Helicase | Helix-turn-helix | Recq | Winged helix | Zn(2+) binding
