2bmu
UMP KINASE FROM PYROCOCCUS FURIOSUS COMPLEXED WITH ITS SUBSTRATE UMP AND ITS SUBSTRATE ANALOG AMPPNP
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OverviewOverview
UMP kinase (UMPK), the enzyme responsible for microbial UMP, phosphorylation, plays a key role in pyrimidine nucleotide biosynthesis, regulating this process via feed-back control and via gene repression of, carbamoyl phosphate synthetase (the first enzyme of the pyrimidine, biosynthesis pathway). We present crystal structures of Pyrococcus, furiosus UMPK, free or complexed with AMPPNP or AMPPNP and UMP, at 2.4 A, 3 A and 2.55 A resolution, respectively, providing a true snapshot of the, catalytically competent bisubstrate complex. The structure proves that, UMPK does not resemble other nucleoside monophosphate kinases, including, the UMP/CMP kinase found in animals, and thus UMPK may be a potential, antimicrobial target. This enzyme has a homohexameric architecture centred, around a ... [(full description)]
About this StructureAbout this Structure
2BMU is a [Single protein] structure of sequence from [Pyrococcus furiosus] with MG, ANP and U5P as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
The crystal structure of Pyrococcus furiosus UMP kinase provides insight into catalysis and regulation in microbial pyrimidine nucleotide biosynthesis., Marco-Marin C, Gil-Ortiz F, Rubio V, J Mol Biol. 2005 Sep 16;352(2):438-54. PMID:16095620
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