1rxq

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Revision as of 02:49, 21 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1rxq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rxq, resolution 1.70Å" /> '''YfiT from Bacillus s...)
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File:1rxq.gif


1rxq, resolution 1.70Å

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YfiT from Bacillus subtilis is a probable metal-dependent hydrolase with an unusual four-helix bundle topology

OverviewOverview

YfiT, a 19-kDa polypeptide from Bacillus subtilis, belongs to a small, sequence family with members predominantly from Gram positive bacteria. We, have determined the crystal structure of YfiT in complex with Ni(2+) to a, resolution of 1.7 A. YfiT exists as a dimer and binds Ni(2+) in a 1:1, stoichiometry. The protein has an unusual four-helix bundle topology and, coordinates Ni(2+) in an octahedral geometry with three conserved, histidines and three waters. Although there is no similarity in their, overall structures, the coordination geometry of the metal and the, residues that constitute the putative active site in YfiT are similar to, those of metalloproteases such as thermolysin. Our structural analyses, suggest that YfiT might function as a metal-dependent hydrolase.

About this StructureAbout this Structure

1RXQ is a Single protein structure of sequence from Bacillus subtilis with NI and GLU as ligands. Full crystallographic information is available from OCA.

ReferenceReference

YfiT from Bacillus subtilis is a probable metal-dependent hydrolase with an unusual four-helix bundle topology., Rajan SS, Yang X, Shuvalova L, Collart F, Anderson WF, Biochemistry. 2004 Dec 14;43(49):15472-9. PMID:15581359

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