1xdo
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Polyphosphate_kinase Polyphosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.1 2.7.4.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Polyphosphate_kinase Polyphosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.1 2.7.4.1] </span> |
|GENE= ppk ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= ppk ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1xdp|1XDP]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xdo OCA], [http://www.ebi.ac.uk/pdbsum/1xdo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xdo RCSB]</span> | ||
}} | }} | ||
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[[Category: ppk]] | [[Category: ppk]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:48:13 2008'' |
Revision as of 21:48, 30 March 2008
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| , resolution 3.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | ppk (Escherichia coli) | ||||||
| Activity: | Polyphosphate kinase, with EC number 2.7.4.1 | ||||||
| Related: | 1XDP
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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