1mkz
From Proteopedia
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. 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 Page seeded by OCA on Sat May 3 01:20:49 2008
Categories: Escherichia coli | Single protein | Edwards, A. | Joachimiak, A. | MCSG, Midwest Center for Structural Genomics. | Sanishvili, R. | Savchenko, A. | Skarina, T. | Mad | Mcsg | Midwest center for structural genomic | Molybdopterin synthesis | Protein structure initiative | Psi | Structural genomic | Weak anomalous signal
