6req
From Proteopedia
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| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | MUTB (Propionibacterium freudenreichii subsp. shermanii), MUTA (Propionibacterium freudenreichii subsp. shermanii) | ||||||
| Activity: | Methylmalonyl-CoA mutase, with EC number 5.4.99.2 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Mon Mar 31 05:43:32 2008
