| Literature DB >> 15269205 |
Ruslan Sanishvili1, Steven Beasley, Tania Skarina, David Glesne, Andrzej Joachimiak, Aled Edwards, Alexei Savchenko.
Abstract
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.Entities:
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Year: 2004 PMID: 15269205 PMCID: PMC3366512 DOI: 10.1074/jbc.M407694200
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157