2faf
From Proteopedia
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[[Image:2faf.gif|left|200px]] | [[Image:2faf.gif|left|200px]] | ||
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'''The structure of chicken mitochondrial PEPCK.''' | '''The structure of chicken mitochondrial PEPCK.''' | ||
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Structural insights into the mechanism of PEPCK catalysis., Holyoak T, Sullivan SM, Nowak T, Biochemistry. 2006 Jul 11;45(27):8254-63. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16819824 16819824] | Structural insights into the mechanism of PEPCK catalysis., Holyoak T, Sullivan SM, Nowak T, Biochemistry. 2006 Jul 11;45(27):8254-63. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16819824 16819824] | ||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
| - | [[Category: Phosphoenolpyruvate carboxykinase (GTP)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Holyoak, T.]] | [[Category: Holyoak, T.]] | ||
[[Category: Nowak, T.]] | [[Category: Nowak, T.]] | ||
[[Category: Sullivan, S M.]] | [[Category: Sullivan, S M.]] | ||
| - | [[Category: | + | [[Category: Kinase]] |
| - | [[Category: | + | [[Category: Pepck]] |
| - | [[Category: | + | [[Category: Phosphoenolpyruvate carboxykinase]] |
| - | [[Category: | + | [[Category: Phosphoryl transfer]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:39:38 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 00:39, 4 May 2008
The structure of chicken mitochondrial PEPCK.
Overview
Phosphoenolpyruvate carboxykinase catalyzes the reversible decarboxylation of oxaloacetic acid with the concomitant transfer of the gamma-phosphate of GTP to form PEP and GDP as the first committed step of gluconeogenesis and glyceroneogenesis. The three structures of the mitochondrial isoform of PEPCK reported are complexed with Mn2+, Mn2+-PEP, or Mn2+-malonate-Mn2+ GDP and provide the first observations of the structure of the mitochondrial isoform and insight into the mechanism of catalysis mediated by this enzyme. The structures show the involvement of the hyper-reactive cysteine (C307) in the coordination of the active site Mn2+. Upon formation of the PEPCK-Mn2+-PEP or PEPCK-Mn2+-malonate-Mn2+ GDP complexes, C307 coordination is lost as the P-loop in which it resides adopts a different conformation. The structures suggest that stabilization of the cysteine-coordinated metal geometry holds the enzyme as a catalytically incompetent metal complex and may represent a previously unappreciated mechanism of regulation. A third conformation of the mobile P-loop in the PEPCK-Mn2+-malonate-Mn2+ GDP complex demonstrates the participation of a previously unrecognized, conserved serine residue (S305) in mediating phosphoryl transfer. The ordering of the mobile active site lid in the PEPCK-Mn2+-malonate-Mn2+ GDP complex yields the first observation of this structural feature and provides additional insight into the mechanism of phosphoryl transfer.
About this Structure
2FAF is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
Structural insights into the mechanism of PEPCK catalysis., Holyoak T, Sullivan SM, Nowak T, Biochemistry. 2006 Jul 11;45(27):8254-63. PMID:16819824 Page seeded by OCA on Sun May 4 03:39:38 2008
