This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1vgq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1vgq.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1vgq.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1vgq| PDB=1vgq | SCENE= }}
{{STRUCTURE_1vgq| PDB=1vgq | SCENE= }}
-
'''Formyl-CoA transferase mutant Asp169 to Ala'''
+
===Formyl-CoA transferase mutant Asp169 to Ala===
-
==Overview==
+
<!--
-
Oxalobacter formigenes is an obligate anaerobe that colonizes the human gastrointestinal tract and employs oxalate breakdown to generate ATP in a novel process involving the interplay of two coupled enzymes and a membrane-bound oxalate:formate antiporter. Formyl-CoA transferase is a critical enzyme in oxalate-dependent ATP synthesis and is the first Class III CoA-transferase for which a high resolution, three-dimensional structure has been determined (Ricagno, S., Jonsson, S., Richards, N., and Lindqvist, Y. (2003) EMBO J. 22, 3210-3219). We now report the first detailed kinetic characterizations of recombinant, wild type formyl-CoA transferase and a number of site-specific mutants, which suggest that catalysis proceeds via a series of anhydride intermediates. Further evidence for this mechanistic proposal is provided by the x-ray crystallographic observation of an acylenzyme intermediate that is formed when formyl-CoA transferase is incubated with oxalyl-CoA. The catalytic mechanism of formyl-CoA transferase is therefore established and is almost certainly employed by all other members of the Class III CoA-transferase family.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15213226}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15213226 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15213226}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Oxalate]]
[[Category: Oxalate]]
[[Category: Oxalate degradation]]
[[Category: Oxalate degradation]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:31:19 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:52:49 2008''

Revision as of 21:52, 28 July 2008

Image:1vgq.png

Template:STRUCTURE 1vgq

Formyl-CoA transferase mutant Asp169 to Ala

Template:ABSTRACT PUBMED 15213226

About this Structure

1VGQ is a Single protein structure of sequence from Oxalobacter formigenes. Full crystallographic information is available from OCA.

Reference

Kinetic and mechanistic characterization of the formyl-CoA transferase from Oxalobacter formigenes., Jonsson S, Ricagno S, Lindqvist Y, Richards NG, J Biol Chem. 2004 Aug 20;279(34):36003-12. Epub 2004 Jun 21. PMID:15213226

Page seeded by OCA on Tue Jul 29 00:52:49 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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