2ie8

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[[Image:2ie8.gif|left|200px]]
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{{Structure
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|PDB= 2ie8 |SIZE=350|CAPTION= <scene name='initialview01'>2ie8</scene>, resolution 1.8&Aring;
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The line below this paragraph, containing "STRUCTURE_2ie8", creates the "Structure Box" on the page.
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <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>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ie8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ie8 OCA], [http://www.ebi.ac.uk/pdbsum/2ie8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ie8 RCSB]</span>
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'''Crystal structure of Thermus caldophilus phosphoglycerate kinase in the open conformation'''
'''Crystal structure of Thermus caldophilus phosphoglycerate kinase in the open conformation'''
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[[Category: Im, Y J.]]
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[[Category: Lee, J H.]]
[[Category: Lee, J H.]]
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[[Category: crystal structure]]
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[[Category: Crystal structure]]
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[[Category: domain movement]]
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[[Category: Domain movement]]
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[[Category: phosphoglycerate kinase]]
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[[Category: Phosphoglycerate kinase]]
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[[Category: thermus caldophilus]]
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[[Category: Thermus caldophilus]]
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Revision as of 04:23, 4 May 2008

Image:2ie8.gif

Template:STRUCTURE 2ie8

Crystal structure of Thermus caldophilus phosphoglycerate kinase in the open conformation


Overview

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.

About this Structure

2IE8 is a Single protein structure of sequence from Thermus caldophilus. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sun May 4 07:23:58 2008

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