1xdo

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{{STRUCTURE_1xdo| PDB=1xdo | SCENE= }}
{{STRUCTURE_1xdo| PDB=1xdo | SCENE= }}
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'''Crystal Structure of Escherichia coli Polyphosphate Kinase'''
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===Crystal Structure of Escherichia coli Polyphosphate Kinase===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15947782 is the PubMed ID number.
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==About this Structure==
==About this Structure==
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[[Category: Polyphosphate kinase]]
[[Category: Polyphosphate kinase]]
[[Category: Ppk]]
[[Category: Ppk]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:23:47 2008''

Revision as of 13:23, 28 July 2008

Image:1xdo.png

Template:STRUCTURE 1xdo

Crystal Structure of Escherichia coli Polyphosphate Kinase

Template:ABSTRACT PUBMED 15947782

About this Structure

1XDO is a Single protein structure of sequence from Escherichia coli. 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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