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| | <StructureSection load='6hxe' size='340' side='right'caption='[[6hxe]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='6hxe' size='340' side='right'caption='[[6hxe]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6hxe]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp._'tac_ii_18' Pseudomonas sp. 'tac ii 18']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HXE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HXE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6hxe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._'TAC_II_18' Pseudomonas sp. 'TAC II 18']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HXE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HXE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene></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]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6i06|6i06]]</td></tr>
| + | <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></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pgk ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=76981 Pseudomonas sp. 'TAC II 18'])</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=6hxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hxe OCA], [https://pdbe.org/6hxe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hxe RCSB], [https://www.ebi.ac.uk/pdbsum/6hxe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hxe ProSAT]</span></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>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6hxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hxe OCA], [http://pdbe.org/6hxe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hxe RCSB], [http://www.ebi.ac.uk/pdbsum/6hxe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hxe ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9RBS3_9PSED Q9RBS3_9PSED] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6hxe" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6hxe" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Phosphoglycerate kinase 3D structures|Phosphoglycerate kinase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Phosphoglycerate kinase]]
| + | [[Category: Pseudomonas sp. 'TAC II 18']] |
| - | [[Category: Pseudomonas sp. 'tac ii 18']] | + | [[Category: Aghajari N]] |
| - | [[Category: Aghajari, N]] | + | [[Category: Haser R]] |
| - | [[Category: Haser, R]] | + | [[Category: Mandelman D]] |
| - | [[Category: Mandelman, D]] | + | |
| - | [[Category: 3-phosphoglycerate]]
| + | |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Hinge binding]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
Q9RBS3_9PSED
Publication Abstract from PubMed
Crystal structures of phosphoglycerate kinase (PGK) from the psychrophile Pseudomonas sp. TACII 18 have been determined at high resolution by X-ray crystallography methods and compared with mesophilic, thermophilic and hyperthermophilic counterparts. PGK is a two-domain enzyme undergoing large domain movements to catalyze the production of ATP from 1,3-biphosphoglycerate and ADP. Whereas the conformational dynamics sustaining the catalytic mechanism of this hinge-bending enzyme now seems rather clear, the determinants which underlie high catalytic efficiency at low temperatures of this psychrophilic PGK were unknown. The comparison of the three-dimensional structures shows that multiple (global and local) specific adaptations have been brought about by this enzyme. Together, these reside in an overall increased flexibility of the cold-adapted PGK thereby allowing a better accessibility to the active site, but also a potentially more disordered transition state of the psychrophilic enzyme, due to the destabilization of some catalytic residues.
Structural determinants increasing flexibility confer cold adaptation in psychrophilic phosphoglycerate kinase.,Mandelman D, Ballut L, Wolff DA, Feller G, Gerday C, Haser R, Aghajari N Extremophiles. 2019 May 30. pii: 10.1007/s00792-019-01102-x. doi:, 10.1007/s00792-019-01102-x. PMID:31147836[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Mandelman D, Ballut L, Wolff DA, Feller G, Gerday C, Haser R, Aghajari N. Structural determinants increasing flexibility confer cold adaptation in psychrophilic phosphoglycerate kinase. Extremophiles. 2019 May 30. pii: 10.1007/s00792-019-01102-x. doi:, 10.1007/s00792-019-01102-x. PMID:31147836 doi:http://dx.doi.org/10.1007/s00792-019-01102-x
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