6hxe: Difference between revisions
m Protected "6hxe" [edit=sysop:move=sysop] |
No edit summary |
||
| Line 1: | Line 1: | ||
==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]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6hxe]] is a 1 chain structure. 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> | |||
</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> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6i06|6i06]]</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> | |||
<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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6hxe" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Phosphoglycerate kinase]] | |||
[[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]] | |||