2faf: Difference between revisions

New page: left|200px<br /><applet load="2faf" size="450" color="white" frame="true" align="right" spinBox="true" caption="2faf, resolution 1.700Å" /> '''The structure of ch...
 
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[[Image:2faf.gif|left|200px]]<br /><applet load="2faf" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2faf.gif|left|200px]]<br /><applet load="2faf" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2faf, resolution 1.700&Aring;" />
caption="2faf, resolution 1.700&Aring;" />
'''The structure of chicken mitochondrial PEPCK.'''<br />
'''The structure of chicken mitochondrial PEPCK.'''<br />


==Overview==
==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.
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==
==About this Structure==
2FAF 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 MN, 20S, EPE and 1PE as [http://en.wikipedia.org/wiki/ligands ligands]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FAF OCA].  
2FAF 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=20S:'>20S</scene>, <scene name='pdbligand=EPE:'>EPE</scene> and <scene name='pdbligand=1PE:'>1PE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=2FAF OCA].  


==Reference==
==Reference==
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[[Category: Holyoak, T.]]
[[Category: Holyoak, T.]]
[[Category: Nowak, T.]]
[[Category: Nowak, T.]]
[[Category: Sullivan, S.M.]]
[[Category: Sullivan, S M.]]
[[Category: 1PE]]
[[Category: 1PE]]
[[Category: 20S]]
[[Category: 20S]]
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[[Category: phosphoryl transfer]]
[[Category: phosphoryl transfer]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:27:11 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:19:22 2008''

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