1xdo
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(New page: 200px<br /><applet load="1xdo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xdo, resolution 3.0Å" /> '''Crystal Structure of ...)
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Revision as of 03:53, 21 November 2007
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Crystal Structure of Escherichia coli Polyphosphate Kinase
Overview
Polyphosphate (polyP), a linear polymer of hundreds of orthophosphate, residues, exists in all tested cells in nature, from pathogenic bacteria, to mammals. In bacteria, polyP has a crucial role in stress responses and, stationary-phase survival. Polyphosphate kinase (PPK) is the principal, enzyme that catalyses the synthesis of polyP in bacteria. It has been, shown that PPK is required for bacterial motility, biofilm formation and, the production of virulence factors. PPK inhibitors may thus provide a, unique therapeutic opportunity against antibiotic-resistant pathogens., Here, we report crystal structures of full-length Escherichia coli PPK and, its complex with AMPPNP (beta-gamma-imidoadenosine 5-phosphate). PPK forms, an interlocked dimer, with each 80 kDa monomer containing four structural, domains. The PPK active site is located in a tunnel, which contains a, unique ATP-binding pocket and may accommodate the translocation of, synthesized polyP. The PPK structure has laid the foundation for, understanding the initiation of polyP synthesis by PPK.
About this Structure
1XDO is a Single protein structure of sequence from Escherichia coli. Active as Polyphosphate kinase, with EC number 2.7.4.1 Full crystallographic information is available from OCA.
Reference
Crystal structure of a polyphosphate kinase and its implications for polyphosphate synthesis., Zhu Y, Huang W, Lee SS, Xu W, EMBO Rep. 2005 Jul;6(7):681-7. PMID:15947782
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