2jjx

From PDBWiki

Authors	Meier, C. Carter, L.G. Sainsbury, S. Mancini, E.J. Owens, R.J. Stuart, D.I. Esnouf, R.M.
Citation	The Crystal Structure of Ump Kinase from Bacillus Anthracis (Ba1797) Reveals an Allosteric Nucleotide-Binding Site. PubMed
Release date	2008-07-29
Exp. Method	X-RAY DIFFRACTION
Resolution	2.82 Å
Classification	TRANSFERASE

Sequence

Chain(s) A B C (255 residues): Blast Uniprot EC 2.7.4.22

MAHHHHHHMRPYKRVLIKLSGGALADQTGNSFNSKRLEHIANEILSIVDLGIEVSIVIGGGNIFRGHLAEEWGIDRVEAD
NIGTLGTIINSLMLRGVLTSKTNKEVRVMTSIPFNAVAEPYIRLRAVHHLDNGYIVIFGGGNGQPFVTTDYPSVQRAIEM
NSDAILVAKQGVDGVFTSDPKHNKSAKMYRKLNYNDVVRQNIQVMDQAALLLARDYNLPAHVFNFDEPGVMRRICLGEHV
GTLINDDASLLVHEK

User comments

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 in a complex fashion by various metabolites (including GTP, Mg2+, ATP, UTP).

From previously solved crystal structures of bacterial UMP kinases, the enzymatic mechanism of the enzyme is well-characterized, but the molecular basis of its regulation is poorly understood.

The crystal structure of UMP kinase from Bacillus anthracis reported here, reveals a previously undiscovered allosteric nucleotide binding site. The site is located near the center of the hexameric structure and is conserved across bacterial (but not archaeal) species.

The existence of this allosteric site sheds light on the molecular basis of regulation of bacterial UMP kinases and may also provide a site for pharmacological intervention.

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