1j9j

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(New page: 200px<br /><applet load="1j9j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j9j, resolution 1.90&Aring;" /> '''CRYSTAL STRUCTURE AN...)
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Revision as of 15:54, 20 November 2007

Image:1j9j.jpg

1j9j, resolution 1.90Å

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CRYSTAL STRUCTURE ANALYSIS OF SURE PROTEIN FROM T.MARITIMA

Overview

Homologs of the Escherichia coli surE gene are present in many eubacteria, and archaea. Despite the evolutionary conservation, little information is, available on the structure and function of their gene products. We have, determined the crystal structure of the SurE protein from Thermotoga, maritima. The structure reveals the dimeric arrangement of the subunits, and an active site around a bound metal ion. We also demonstrate that the, SurE protein exhibits a divalent metal ion-dependent phosphatase activity, that is inhibited by vanadate or tungstate. In the vanadate- and, tungstate-complexed structures, the inhibitors bind adjacent to the, divalent metal ion. Our structural and functional analyses identify the, SurE proteins as a novel family of metal ion-dependent phosphatases.

About this Structure

1J9J is a Single protein structure of sequence from Thermotoga maritima with MG and SO4 as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure and functional analysis of the SurE protein identify a novel phosphatase family., Lee JY, Kwak JE, Moon J, Eom SH, Liong EC, Pedelacq JD, Berendzen J, Suh SW, Nat Struct Biol. 2001 Sep;8(9):789-94. PMID:11524683

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