The crystal structure of UMP kinase from Bacillus anthracis (BA1797) reveals an allosteric nucleotide-binding site.

Journal article

Uridine monophosphate (UMP) kinase is a conserved enzyme that catalyzes the ATP-driven conversion of uridylate monophosphate into uridylate diphosphate, an essential metabolic step. In prokaryotes, the enzyme exists as a homohexamer that is regulated by various metabolites. Whereas the enzymatic mechanism of UMP kinase (UK) is well-characterized, the molecular basis of its regulation remains poorly understood. Here we report the crystal structure of UK from Bacillus anthracis (BA1797) in comp...

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Authors: Meier, C; Carter, L; Sainsbury, S; Mancini, E; Owens, R

• Publication status: Published
• Journal: Journal of molecular biology
• Volume: 381
• Issue: 5
• Pages: 1098-1105
• Publication date: 2008-09-01
• DOI: 10.1016/j.jmb.2008.06.078
• EISSN: 1089-8638
• ISSN: 0022-2836
• Language: English
• Keywords: Allosteric Site; Protein Structure, Quaternary; Crystallography, X-Ray; Coenzymes; Nucleotides; Eukaryotic Cells; Bacillus anthracis; Molecular Sequence Data; Protein Structure, Secondary; Nucleoside-Phosphate Kinase; Models, Molecular; Amino Acid Sequence; Prokaryotic Cells