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13pk

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(New page: {{Seed}} 200px <!-- The line below this paragraph, containing "STRUCTURE_13pk", creates the "Structure Box" on the page. You may change the PDB parameter (which se...)
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[[Image:13pk.png|left|200px]]
 
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==TERNARY COMPLEX OF PHOSPHOGLYCERATE KINASE FROM TRYPANOSOMA BRUCEI==
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The line below this paragraph, containing "STRUCTURE_13pk", creates the "Structure Box" on the page.
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<StructureSection load='13pk' size='340' side='right'caption='[[13pk]], [[Resolution|resolution]] 2.50&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'>[[13pk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_brucei Trypanosoma brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=13PK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=13PK 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]] 2.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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{{STRUCTURE_13pk| PDB=13pk | SCENE= }}
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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=13pk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=13pk OCA], [https://pdbe.org/13pk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=13pk RCSB], [https://www.ebi.ac.uk/pdbsum/13pk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=13pk ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PGKC_TRYBB PGKC_TRYBB]
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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/3p/13pk_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=13pk 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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Phosphoglycerate kinase (PGK), a key enzyme in glycolysis, catalyses the transfer of a phosphoryl-group from 1,3-bisphosphoglycerate to ADP to form 3-phosphoglycerate and ATP. Despite extensive kinetic and structural investigations over more than two decades, the conformation assumed by this enzyme during catalysis remained unknown. Here we present the 2.8 A crystal structure of a ternary complex of PGK from Trypanosoma brucei, the causative agent of sleeping sickness. This structure determination relied on a procedure in which fragments containing less than 10% of the scattering mass were successively positioned in the unit cell to obtain phases. The PGK ternary complex exhibits a dramatic closing of the large cleft between the two domains seen in all previous studies, thereby bringing the two ligands, 3-phosphoglycerate and ADP into close proximity. Our results demonstrate that PGK is a hinge-bending enzyme, reveal a novel mechanism in which substrate-induced effects combine synergistically to induce major conformational changes and, to our knowledge, afford the first observation of the PGK active site in a catalytic conformation.
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===TERNARY COMPLEX OF PHOSPHOGLYCERATE KINASE FROM TRYPANOSOMA BRUCEI===
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Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activation.,Bernstein BE, Michels PA, Hol WG Nature. 1997 Jan 16;385(6613):275-8. PMID:9000079<ref>PMID:9000079</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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<div class="pdbe-citations 13pk" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Phosphoglycerate kinase 3D structures|Phosphoglycerate kinase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 9000079 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_9000079}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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13PK is a 4 chains structure with sequences from [http://en.wikipedia.org/wiki/Trypanosoma_brucei Trypanosoma brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=13PK OCA].
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==Reference==
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<ref group="xtra">PMID:9000079</ref><references group="xtra"/>
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[[Category: Phosphoglycerate kinase]]
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[[Category: Trypanosoma brucei]]
[[Category: Trypanosoma brucei]]
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[[Category: Bernstein, B E.]]
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[[Category: Bernstein BE]]
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[[Category: Hol, W G.J.]]
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[[Category: Hol WGJ]]
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[[Category: Michels, P A.M.]]
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[[Category: Michels PAM]]
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[[Category: Glycolysis]]
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[[Category: Kinase]]
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[[Category: Phosphoglycerate]]
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[[Category: Ternary complex]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 16 23:07:10 2010''
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Current revision

TERNARY COMPLEX OF PHOSPHOGLYCERATE KINASE FROM TRYPANOSOMA BRUCEI

PDB ID 13pk

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