1mkz

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(New page: 200px<br /><applet load="1mkz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mkz, resolution 1.60&Aring;" /> '''Crystal structure of...)
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Revision as of 19:22, 20 November 2007

Image:1mkz.jpg

1mkz, resolution 1.60Å

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Crystal structure of MoaB protein at 1.6 A resolution.

Overview

The crystal structure of Escherichia coli MoaB was determined by, multiwavelength anomalous diffraction phasing and refined at 1.6-A, resolution. The molecule displayed a modified Rossman fold. MoaB is, assembled into a hexamer composed of two trimers. The monomers have high, structural similarity with two proteins, MogA and MoeA, from the, molybdenum cofactor synthesis pathway in E. coli, as well as with domains, of mammalian gephyrin and plant Cnx1, which are also involved in, molybdopterin synthesis. Structural comparison between these proteins and, the amino acid conservation patterns revealed a putative active site in, MoaB. The structural analysis of this site allowed to advance several, hypothesis that can be tested in further studies.

About this Structure

1MKZ is a Single protein structure of sequence from Escherichia coli with SO4 and ACY as ligands. Full crystallographic information is available from OCA.

Reference

The crystal structure of Escherichia coli MoaB suggests a probable role in molybdenum cofactor synthesis., Sanishvili R, Beasley S, Skarina T, Glesne D, Joachimiak A, Edwards A, Savchenko A, J Biol Chem. 2004 Oct 1;279(40):42139-46. Epub 2004 Jul 21. PMID:15269205

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