2ie8
From Proteopedia
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| - | [[Image:2ie8.gif|left|200px]]<br /><applet load="2ie8" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2ie8, resolution 1.8Å" /> | ||
| - | '''Crystal structure of Thermus caldophilus phosphoglycerate kinase in the open conformation'''<br /> | ||
| - | == | + | ==Crystal structure of Thermus caldophilus phosphoglycerate kinase in the open conformation== |
| + | <StructureSection load='2ie8' size='340' side='right'caption='[[2ie8]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2ie8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_caldophilus Thermus caldophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IE8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IE8 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ie8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ie8 OCA], [https://pdbe.org/2ie8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ie8 RCSB], [https://www.ebi.ac.uk/pdbsum/2ie8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ie8 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q08GC7_THECA Q08GC7_THECA] | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ie/2ie8_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=2ie8 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
Phosphoglycerate kinase (PGK) is a key glycolytic enzyme that catalyzes the reversible transfer of a phosphate from 1,3-bisphosphoglycerate to ADP to form 3-phosphoglycerate and ATP in the presence of magnesium. During catalysis, a conformational change occurs that brings the N- and C-domains of PGK closer together. Here we present the 1.8A crystal structure of unliganded PGK from Thermus caldophilus (Tca). Comparison of the structure of TcaPGK (open conformation) with that of Thermotoga maritima (Tma) PGK (closed conformation) revealed that the conformational change reflects a change in the interaction between the domains. We identified Arg148 as a key residue involved in open-to-closed transition. The open conformation of TcaPGK is stabilized by an interdomain salt bridge between Arg148 and Glu375. The binding of 3-PG (or maybe 1,3-BPG) disrupts this salt bridge and, in ternary complex, the formation of new salt bridge between Arg60 and Asp197 stabilizes the closed conformation. | Phosphoglycerate kinase (PGK) is a key glycolytic enzyme that catalyzes the reversible transfer of a phosphate from 1,3-bisphosphoglycerate to ADP to form 3-phosphoglycerate and ATP in the presence of magnesium. During catalysis, a conformational change occurs that brings the N- and C-domains of PGK closer together. Here we present the 1.8A crystal structure of unliganded PGK from Thermus caldophilus (Tca). Comparison of the structure of TcaPGK (open conformation) with that of Thermotoga maritima (Tma) PGK (closed conformation) revealed that the conformational change reflects a change in the interaction between the domains. We identified Arg148 as a key residue involved in open-to-closed transition. The open conformation of TcaPGK is stabilized by an interdomain salt bridge between Arg148 and Glu375. The binding of 3-PG (or maybe 1,3-BPG) disrupts this salt bridge and, in ternary complex, the formation of new salt bridge between Arg60 and Asp197 stabilizes the closed conformation. | ||
| - | + | Crystal structure of Thermus caldophilus phosphoglycerate kinase in the open conformation.,Lee JH, Im YJ, Bae J, Kim D, Kim MK, Kang GB, Lee DS, Eom SH Biochem Biophys Res Commun. 2006 Dec 1;350(4):1044-9. Epub 2006 Oct 6. PMID:17045964<ref>PMID:17045964</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2ie8" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Phosphoglycerate kinase 3D structures|Phosphoglycerate kinase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thermus caldophilus]] | ||
| + | [[Category: Eom SH]] | ||
| + | [[Category: Im YJ]] | ||
| + | [[Category: Lee JH]] | ||
Current revision
Crystal structure of Thermus caldophilus phosphoglycerate kinase in the open conformation
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