6req
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="6req" size="450" color="white" frame="true" align="right" spinBox="true" caption="6req, resolution 2.20Å" /> '''METHYLMALONYL-COA MU...)
Next diff →
Revision as of 13:18, 20 November 2007
|
METHYLMALONYL-COA MUTASE, 3-CARBOXYPROPYL-COA INHIBITOR COMPLEX
Overview
X-ray crystal structures of methylmalonyl-CoA mutase in complexes with, substrate methylmalonyl-CoA and inhibitors 2-carboxypropyl-CoA and, 3-carboxypropyl-CoA (substrate and product analogues) show that the, enzyme-substrate interactions change little during the course of the, rearrangement reaction, in contrast to the large conformational change on, substrate binding. The substrate complex shows a 5'-deoxyadenine molecule, in the active site, bound weakly and not attached to the cobalt atom of, coenzyme B12, rotated and shifted from its position in the substrate-free, adenosylcobalamin complex. The position of Tyralpha89 close to the, substrate explains the stereochemical selectivity of the enzyme for, (2R)-methylmalonyl-CoA.
About this Structure
6REQ is a Protein complex structure of sequences from Propionibacterium freudenreichii subsp. shermanii with 3CP, B12 and GOL as ligands. Active as Methylmalonyl-CoA mutase, with EC number 5.4.99.2 Full crystallographic information is available from OCA.
Reference
Crystal structure of substrate complexes of methylmalonyl-CoA mutase., Mancia F, Smith GA, Evans PR, Biochemistry. 1999 Jun 22;38(25):7999-8005. PMID:10387043
Page seeded by OCA on Tue Nov 20 15:25:39 2007
