1k3c: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:1k3c.jpg|left|200px]]
{{Seed}}
[[Image:1k3c.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1k3c|  PDB=1k3c  |  SCENE=  }}  
{{STRUCTURE_1k3c|  PDB=1k3c  |  SCENE=  }}  


'''Phosphoenolpyruvate carboxykinase in complex with ADP, AlF3 and Pyruvate'''
===Phosphoenolpyruvate carboxykinase in complex with ADP, AlF3 and Pyruvate===




==Overview==
<!--
The mechanism of reversible transfer of the gamma-phosphate group of ATP by Escherichia coli phosphoenolpyruvate carboxykinase (PCK) on to its substrate is of great interest. It is known that metallofluorides are accurate analogs of the transition state in the context of kinase mechanisms. Therefore, two complexes of PCK, one with AlF(3), Mg(2+) and ADP (complex I), the other with AlF(3), Mg(2+), ADP and pyruvate (complex II) were crystallized. The X-ray crystal structures of these two complexes were determined at 2.0 A resolution. The Al atom has trigonal bipyramidal geometry that mimics the transition state of phosphoryl transfer. The Al atom is at a distance of 2.8 A and 2.9 A from an oxygen atom of the beta-phosphoryl group of ADP in complex I and II, respectively. A water molecule in complex I and an oxygen atom of the pyruvate in complex II are located along the axis of the trigonal bipyramid on the side opposite to the beta-phosphoryl oxygen with respect to the equatorial plane, suggesting that the complexes are close mimics of the transition state. Along with the presence of positively charged species around the AlF(3) moiety, these results indicate that phosphoryl transfer occurs via a direct displacement mechanism with associative qualities.
The line below this paragraph, {{ABSTRACT_PUBMED_11724534}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 11724534 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_11724534}}


==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Nucleotide-triphosphate hydrolase]]
[[Category: Nucleotide-triphosphate hydrolase]]
[[Category: P-loop]]
[[Category: P-loop]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 22:15:03 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:24:49 2008''

Revision as of 12:24, 28 July 2008

File:1k3c.png

Template:STRUCTURE 1k3c

Phosphoenolpyruvate carboxykinase in complex with ADP, AlF3 and Pyruvate

Template:ABSTRACT PUBMED 11724534

About this Structure

1K3C is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The phosphoryl-transfer mechanism of Escherichia coli phosphoenolpyruvate carboxykinase from the use of AlF(3)., Sudom AM, Prasad L, Goldie H, Delbaere LT, J Mol Biol. 2001 Nov 16;314(1):83-92. PMID:11724534

Page seeded by OCA on Mon Jul 28 15:24:49 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1k3c&oldid=704740"