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.


1p5h

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1p5h.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1p5h.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1p5h| PDB=1p5h | SCENE= }}
{{STRUCTURE_1p5h| PDB=1p5h | SCENE= }}
-
'''Crystal structure of Formyl-CoA Transferase (apoenzyme) from Oxalobacter formigenes'''
+
===Crystal structure of Formyl-CoA Transferase (apoenzyme) from Oxalobacter formigenes===
-
==Overview==
+
<!--
-
Formyl-CoA transferase catalyses transfer of CoA from formate to oxalate in the first step of oxalate degradation by Oxalobacter formigenes, a bacterium present in the intestinal flora which is implicated in oxalate catabolism in mammals. Formyl-CoA transferase is a member of a family of CoA-transferases for which no structural information is available. We now report the three-dimensional structure of O.formigenes formyl-CoA transferase, which reveals a novel fold and a very striking assembly of the homodimer. The subunit is composed of a large and a small domain where residues from both the N- and C-termini of the subunit are part of the large domain. The linkers between the domains give the subunit a circular shape with a hole in the middle. The enzyme monomers are tightly interacting and are interlocked. This fold requires drastic rearrangement of approximately 75 residues at the C-terminus for formation of the dimer. The structure of a complex of formyl-CoA transferase with CoA is also reported and sets the scene for a mechanistic understanding of enzymes of this family of CoA-transferases.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12839984}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12839984 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12839984}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Oxalate]]
[[Category: Oxalate]]
[[Category: Oxalate degradation]]
[[Category: Oxalate degradation]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:42:41 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:57:46 2008''

Revision as of 17:57, 28 July 2008

Image:1p5h.png

Template:STRUCTURE 1p5h

Crystal structure of Formyl-CoA Transferase (apoenzyme) from Oxalobacter formigenes

Template:ABSTRACT PUBMED 12839984

About this Structure

1P5H is a Single protein structure of sequence from Oxalobacter formigenes. Full crystallographic information is available from OCA.

Reference

Formyl-CoA transferase encloses the CoA binding site at the interface of an interlocked dimer., Ricagno S, Jonsson S, Richards N, Lindqvist Y, EMBO J. 2003 Jul 1;22(13):3210-9. PMID:12839984

Page seeded by OCA on Mon Jul 28 20:57:46 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1p5h"
Personal tools