6hxe: Difference between revisions

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OCA

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-'''Unreleased structure'''
-The entry 6hxe is ON HOLD
+==Crystal structure of psychrophilic phosphoglycerate kinase from Pseudomonas TACII18 in complex with 3-phosphoglycerate==
+<StructureSection load='6hxe' size='340' side='right'caption='[[6hxe]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+== Structural highlights ==
+<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</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='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>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q9RBS3_9PSED Q9RBS3_9PSED]
+<div style="background-color:#fffaf0;">
+== 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.
-Authors: Mandelman, D., Haser, R., Aghajari, N.
+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<ref>PMID:31147836</ref>
-Description: Crystal structure of psychrophilic phosphoglycerate kinase from Pseudomonas TACII18 in complex with 3-phosphoglycerate
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Haser, R]]
+<div class="pdbe-citations 6hxe" style="background-color:#fffaf0;"></div>
-[[Category: Aghajari, N]]
-[[Category: Mandelman, D]]
+==See Also==
+*[[Phosphoglycerate kinase 3D structures|Phosphoglycerate kinase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Pseudomonas sp. 'TAC II 18']]
+[[Category: Aghajari N]]
+[[Category: Haser R]]
+[[Category: Mandelman D]]