1xdo

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{{Seed}}
 
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[[Image:1xdo.png|left|200px]]
 
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==Crystal Structure of Escherichia coli Polyphosphate Kinase==
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The line below this paragraph, containing "STRUCTURE_1xdo", creates the "Structure Box" on the page.
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<StructureSection load='1xdo' size='340' side='right'caption='[[1xdo]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1xdo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XDO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XDO FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xdo OCA], [https://pdbe.org/1xdo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xdo RCSB], [https://www.ebi.ac.uk/pdbsum/1xdo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xdo ProSAT]</span></td></tr>
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{{STRUCTURE_1xdo| PDB=1xdo | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PPK1_ECOLI PPK1_ECOLI] Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP). Can form linear polymers of orthophosphate with chain lengths up to 1000 or more. Can use GTP instead of ATP, but the efficiency of GTP is 5% that of ATP. Also exhibits several other enzymatic activities, which include: ATP synthesis from polyP in the presence of excess ADP, general nucleoside-diphosphate kinase activity, linear guanosine 5'-tetraphosphate (ppppG) synthesis and autophosphorylation.<ref>PMID:10660553</ref> <ref>PMID:8962061</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xd/1xdo_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xdo ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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===Crystal Structure of Escherichia coli Polyphosphate Kinase===
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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<ref>PMID:15947782</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_15947782}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1xdo" style="background-color:#fffaf0;"></div>
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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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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15947782}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1XDO is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XDO OCA].
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==Reference==
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<ref group="xtra">PMID:15947782</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Polyphosphate kinase]]
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[[Category: Large Structures]]
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[[Category: Huang, W.]]
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[[Category: Huang W]]
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[[Category: Lee, S S.]]
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[[Category: Lee SS]]
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[[Category: Xu, W.]]
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[[Category: Xu W]]
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[[Category: Zhu, Y.]]
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[[Category: Zhu Y]]
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[[Category: E coli polyphosphate kinase]]
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[[Category: Polyphosphate kinase]]
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[[Category: Ppk]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 12:08:36 2009''
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Current revision

Crystal Structure of Escherichia coli Polyphosphate Kinase

PDB ID 1xdo

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