2qzy

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[[Image:2qzy.jpg|left|200px]]<br /><applet load="2qzy" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2qzy.jpg|left|200px]]
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caption="2qzy, resolution 1.9&Aring;" />
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'''The structure of chicken mitochondrial PEPCK in complex with PEP'''<br />
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{{Structure
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|PDB= 2qzy |SIZE=350|CAPTION= <scene name='initialview01'>2qzy</scene>, resolution 1.9&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PEP:PHOSPHOENOLPYRUVATE'>PEP</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene> and <scene name='pdbligand=20S:BETA-D-FRUCTOFURANOSYL 6-O-OCTANOYL-ALPHA-D-GLUCOPYRANOSIDE'>20S</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Phosphoenolpyruvate_carboxykinase_(GTP) Phosphoenolpyruvate carboxykinase (GTP)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.32 4.1.1.32]
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|GENE=
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}}
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'''The structure of chicken mitochondrial PEPCK in complex with PEP'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2QZY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=PEP:'>PEP</scene>, <scene name='pdbligand=EPE:'>EPE</scene> and <scene name='pdbligand=20S:'>20S</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 2FAG. Active as [http://en.wikipedia.org/wiki/Phosphoenolpyruvate_carboxykinase_(GTP) Phosphoenolpyruvate carboxykinase (GTP)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.32 4.1.1.32] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QZY OCA].
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2QZY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. This structure supersedes the now removed PDB entry 2FAG. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QZY OCA].
==Reference==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16819824 16819824]
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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]
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Phosphoenolpyruvate carboxykinase (GTP)]]
[[Category: Phosphoenolpyruvate carboxykinase (GTP)]]
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[[Category: transit peptide]]
[[Category: transit peptide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:43:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:31:15 2008''

Revision as of 16:31, 20 March 2008

Image:2qzy.jpg


PDB ID 2qzy

Drag the structure with the mouse to rotate
, resolution 1.9Å
Ligands: , , and
Activity: Phosphoenolpyruvate carboxykinase (GTP), with EC number 4.1.1.32
Coordinates: save as pdb, mmCIF, xml



The structure of chicken mitochondrial PEPCK in complex with PEP


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

2QZY is a Single protein structure of sequence from Gallus gallus. This structure supersedes the now removed PDB entry 2FAG. 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 Thu Mar 20 18:31:15 2008

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