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1pvu

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(New page: 200px<br /><applet load="1pvu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pvu, resolution 2.4&Aring;" /> '''THE CRYSTAL STRUCTURE...)
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Revision as of 22:02, 20 November 2007


1pvu, resolution 2.4Å

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THE CRYSTAL STRUCTURE OF PVUII ENDONUCLEASE REVEALS EXTENSIVE STRUCTURAL HOMOLOGIES TO ECORV

Overview

The crystal structure of the dimeric PvuII restriction endonuclease, (R.PvuII) has been determined at a resolution of 2.4A. The protein has a, mixed alpha/beta architecture and consists of two subdomains. Despite a, lack of sequence homology, extensive structural similarities exist between, one R.PvuII subdomain and the DNA-binding subdomain of EcoRV endonuclease, (R.EcoRV); the dimerization subdomains are unrelated. Within the similar, domains, flexible segments of R.PvuII are topologically equivalent to the, DNA-binding turns of R.EcoRV; potential catalytic residues can be deduced, from the structural similarities to R.EcoRV. Conformational flexibility is, important for the interaction with DNA. A possible classification of, endonuclease structures on the basis of the positions of the scissile, phosphates is discussed.

About this Structure

1PVU is a Single protein structure of sequence from Proteus vulgaris. Active as Type II site-specific deoxyribonuclease, with EC number 3.1.21.4 Full crystallographic information is available from OCA.

Reference

Crystal structure of PvuII endonuclease reveals extensive structural homologies to EcoRV., Athanasiadis A, Vlassi M, Kotsifaki D, Tucker PA, Wilson KS, Kokkinidis M, Nat Struct Biol. 1994 Jul;1(7):469-75. PMID:7664066

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