1mkz
From Proteopedia
Crystal structure of MoaB protein at 1.6 A resolution.
Structural highlights
FunctionMOAB_ECOLI May be involved in the biosynthesis of molybdopterin. Can bind GTP and has low GTPase activity. Can bind MPT, but has no MPT adenylyl transferase activity.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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