1mkz: Difference between revisions

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[[Image:1mkz.jpg|left|200px]]
{{Seed}}
[[Image:1mkz.png|left|200px]]


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{{STRUCTURE_1mkz|  PDB=1mkz  |  SCENE=  }}  
{{STRUCTURE_1mkz|  PDB=1mkz  |  SCENE=  }}  


'''Crystal structure of MoaB protein at 1.6 A resolution.'''
===Crystal structure of MoaB protein at 1.6 A resolution.===




==Overview==
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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.
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{{ABSTRACT_PUBMED_15269205}}


==About this Structure==
==About this Structure==
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[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: Weak anomalous signal]]
[[Category: Weak anomalous signal]]
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Revision as of 21:13, 2 July 2008

File:1mkz.png

Template:STRUCTURE 1mkz

Crystal structure of MoaB protein at 1.6 A resolution.

Template:ABSTRACT PUBMED 15269205

About this Structure

1MKZ is a Single protein structure of sequence from Escherichia coli. 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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