1MKZ
Crystal structure of MoaB protein at 1.6 A resolution.
Summary for 1MKZ
| Entry DOI | 10.2210/pdb1mkz/pdb |
| Descriptor | Molybdenum cofactor biosynthesis protein B, SULFATE ION, ACETIC ACID, ... (4 entities in total) |
| Functional Keywords | mad, weak anomalous signal, molybdopterin synthesis, structural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg, biosynthetic protein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 38730.33 |
| Authors | Sanishvili, R.,Skarina, T.,Joachimiak, A.,Edwards, A.,Savchenko, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2002-08-29, release date: 2003-04-22, Last modification date: 2024-11-06) |
| Primary citation | Sanishvili, R.,Beasley, S.,Skarina, T.,Glesne, D.,Joachimiak, A.,Edwards, A.,Savchenko, A. The crystal structure of Escherichia coli MoaB suggests a probable role in molybdenum cofactor synthesis. J.Biol.Chem., 279:42139-42146, 2004 Cited by PubMed 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. PubMed: 15269205DOI: 10.1074/jbc.M407694200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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