2bnf
From Proteopedia
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THE STRUCTURE OF E. COLI UMP KINASE IN COMPLEX WITH UTP
Overview
Bacterial UMP kinases are essential enzymes involved in the multistep, synthesis of nucleoside triphosphates. They are hexamers regulated by the, allosteric activator GTP and inhibited by UTP. We solved the crystal, structure of Escherichia coli UMP kinase bound to the UMP substrate (2.3 A, resolution), the UDP product (2.6 A), or UTP (2.45 A). The monomer fold, unrelated to that of other nucleoside monophosphate kinases, belongs to, the carbamate kinase-like superfamily. However, the phosphate acceptor, binding cleft and subunit assembly are characteristic of UMP kinase., Interactions with UMP explain the high specificity for this natural, substrate. UTP, previously described as an allosteric inhibitor, was, unexpectedly found in the phosphate acceptor site, suggesting that it acts, as a ... [(full description)]
About this Structure
2BNF is a [Single protein] structure of sequence from [Escherichia coli] with UTP and GOL as [ligands]. Active as [Nucleoside-phosphate kinase], with EC number [2.7.4.4]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Structure of Escherichia coli UMP kinase differs from that of other nucleoside monophosphate kinases and sheds new light on enzyme regulation., Briozzo P, Evrin C, Meyer P, Assairi L, Joly N, Barzu O, Gilles AM, J Biol Chem. 2005 Jul 8;280(27):25533-40. Epub 2005 Apr 27. PMID:15857829
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