We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1yvy

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1yvy.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1yvy.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1yvy| PDB=1yvy | SCENE= }}
{{STRUCTURE_1yvy| PDB=1yvy | SCENE= }}
-
'''Crystal strucutre of Anaerobiospirillum succiniciproducens phosphoenolpyruvate carboxykinase'''
+
===Crystal strucutre of Anaerobiospirillum succiniciproducens phosphoenolpyruvate carboxykinase===
-
==Overview==
+
<!--
-
The 2.2 Angstroms resolution crystal structure of the enzyme phosphoenolpyruvate carboxykinase (PCK) from the bacterium Anaerobiospirillum succiniciproducens complexed with ATP, Mg(2+), Mn(2+) and the transition state analogue oxalate has been solved. The 2.4 Angstroms resolution native structure of A. succiniciproducens PCK has also been determined. It has been found that upon binding of substrate, PCK undergoes a conformational change. Two domains of the molecule fold towards each other, with the substrates and metal ions held in a cleft formed between the two domains. This domain movement is believed to accelerate the reaction PCK catalyzes by forcing bulk solvent molecules out of the active site. Although the crystal structure of A. succiniciproducens PCK with bound substrate and metal ions is related to the structures of PCK from Escherichia coli and Trypanosoma cruzi, it is the first crystal structure from this class of enzymes that clearly shows an important surface loop (residues 383-397) from the C-terminal domain, hydrogen bonding with the peptide backbone of the active site residue Arg60. The interaction between the surface loop and the active site backbone, which is a parallel beta-sheet, seems to be a feature unique of A. succiniciproducens PCK. The association between the loop and the active site is the third type of interaction found in PCK that is thought to play a part in the domain closure. This loop also appears to help accelerate catalysis by functioning as a 'lid' that shields water molecules from the active site.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15890557}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15890557 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15890557}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: P-loop]]
[[Category: P-loop]]
[[Category: Succinate]]
[[Category: Succinate]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:51:37 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:21:22 2008''

Revision as of 13:21, 27 July 2008

Image:1yvy.png

Template:STRUCTURE 1yvy

Crystal strucutre of Anaerobiospirillum succiniciproducens phosphoenolpyruvate carboxykinase

Template:ABSTRACT PUBMED 15890557

About this Structure

1YVY is a Single protein structure of sequence from Anaerobiospirillum succiniciproducens. Full crystallographic information is available from OCA.

Reference

Crystal structure of Anaerobiospirillum succiniciproducens PEP carboxykinase reveals an important active site loop., Cotelesage JJ, Prasad L, Zeikus JG, Laivenieks M, Delbaere LT, Int J Biochem Cell Biol. 2005 Sep;37(9):1829-37. PMID:15890557

Page seeded by OCA on Sun Jul 27 16:21:22 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1yvy"
Personal tools