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Updated: Aug 23, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
The crystal structure of Escherichia coli MoaB suggests a probable role in molybdenum cofactor synthesis
Ruslan Sanishvili1, Steven Beasley, Tania Skarina
1Biosciences, Structural Biology Center, Midwest Center for Sructural Genomics, Argonne National Laboratory, Argonne, Illinois 60439, USA.
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.
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