1xdp
From Proteopedia
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|PDB= 1xdp |SIZE=350|CAPTION= <scene name='initialview01'>1xdp</scene>, resolution 2.50Å | |PDB= 1xdp |SIZE=350|CAPTION= <scene name='initialview01'>1xdp</scene>, resolution 2.50Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
| - | |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=[[1xdo|1XDO]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xdp OCA], [http://www.ebi.ac.uk/pdbsum/1xdp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xdp RCSB]</span> | ||
}} | }} | ||
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[[Category: Xu, W.]] | [[Category: Xu, W.]] | ||
[[Category: Zhu, Y.]] | [[Category: Zhu, Y.]] | ||
| - | [[Category: ATP]] | ||
| - | [[Category: MG]] | ||
[[Category: amppnp]] | [[Category: amppnp]] | ||
[[Category: e coli polyphosphate kinase]] | [[Category: e coli polyphosphate kinase]] | ||
| Line 34: | Line 35: | ||
[[Category: ppk complex with amppnp]] | [[Category: ppk complex with amppnp]] | ||
| - | ''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
| |||||||
| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | ppk (Escherichia coli) | ||||||
| Activity: | Polyphosphate kinase, with EC number 2.7.4.1 | ||||||
| Related: | 1XDO
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of the E.coli Polyphosphate Kinase in complex with AMPPNP
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
1XDP 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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