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| | <StructureSection load='2ie8' size='340' side='right'caption='[[2ie8]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='2ie8' size='340' side='right'caption='[[2ie8]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ie8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"thermus_caldophilus"_taguchi_et_al._1983 "thermus caldophilus" taguchi et al. 1983]. 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 [http://proteopedia.org/fgij/fg.htm?mol=2IE8 FirstGlance]. <br> | + | <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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoglycerate_kinase Phosphoglycerate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.3 2.7.2.3] </span></td></tr> | + | </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'>[http://proteopedia.org/fgij/fg.htm?mol=2ie8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ie8 OCA], [http://pdbe.org/2ie8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ie8 RCSB], [http://www.ebi.ac.uk/pdbsum/2ie8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ie8 ProSAT]</span></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> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q08GC7_THECA Q08GC7_THECA] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Thermus caldophilus taguchi et al. 1983]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Phosphoglycerate kinase]] | |
| - | [[Category: Eom, S H]] | |
| - | [[Category: Im, Y J]] | |
| - | [[Category: Lee, J H]] | |
| - | [[Category: Domain movement]] | |
| | [[Category: Thermus caldophilus]] | | [[Category: Thermus caldophilus]] |
| - | [[Category: Transferase]] | + | [[Category: Eom SH]] |
| | + | [[Category: Im YJ]] |
| | + | [[Category: Lee JH]] |
| Structural highlights
Function
Q08GC7_THECA
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lee JH, Im YJ, Bae J, Kim D, Kim MK, Kang GB, Lee DS, Eom SH. Crystal structure of Thermus caldophilus phosphoglycerate kinase in the open conformation. Biochem Biophys Res Commun. 2006 Dec 1;350(4):1044-9. Epub 2006 Oct 6. PMID:17045964 doi:10.1016/j.bbrc.2006.09.151
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