2ie8
From Proteopedia
(New page: 200px<br /><applet load="2ie8" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ie8, resolution 1.8Å" /> '''Crystal structure of ...) |
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| - | [[Image:2ie8.gif|left|200px]]<br /><applet load="2ie8" size=" | + | [[Image:2ie8.gif|left|200px]]<br /><applet load="2ie8" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ie8, resolution 1.8Å" /> | caption="2ie8, resolution 1.8Å" /> | ||
'''Crystal structure of Thermus caldophilus phosphoglycerate kinase in the open conformation'''<br /> | '''Crystal structure of Thermus caldophilus phosphoglycerate kinase in the open conformation'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Phosphoglycerate kinase (PGK) is a key glycolytic enzyme that catalyzes | + | 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== | ==About this Structure== | ||
| - | 2IE8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_caldophilus Thermus caldophilus]. Active as [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] Full crystallographic information is available from [http:// | + | 2IE8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_caldophilus Thermus caldophilus]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IE8 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermus caldophilus]] | [[Category: Thermus caldophilus]] | ||
| - | [[Category: Eom, S | + | [[Category: Eom, S H.]] |
| - | [[Category: Im, Y | + | [[Category: Im, Y J.]] |
| - | [[Category: Lee, J | + | [[Category: Lee, J H.]] |
[[Category: crystal structure]] | [[Category: crystal structure]] | ||
[[Category: domain movement]] | [[Category: domain movement]] | ||
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[[Category: thermus caldophilus]] | [[Category: thermus caldophilus]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:51:47 2008'' |
Revision as of 15:51, 21 February 2008
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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. Active as Phosphoglycerate kinase, with EC number 2.7.2.3 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
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