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6req
From Proteopedia
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[[Image:6req.gif|left|200px]] | [[Image:6req.gif|left|200px]] | ||
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'''METHYLMALONYL-COA MUTASE, 3-CARBOXYPROPYL-COA INHIBITOR COMPLEX''' | '''METHYLMALONYL-COA MUTASE, 3-CARBOXYPROPYL-COA INHIBITOR COMPLEX''' | ||
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[[Category: Evans, P R.]] | [[Category: Evans, P R.]] | ||
[[Category: Mancia, F.]] | [[Category: Mancia, F.]] | ||
| - | [[Category: | + | [[Category: Intramolecular transferase]] |
| - | [[Category: | + | [[Category: Isomerase]] |
| - | [[Category: | + | [[Category: Mutase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:42:42 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 19:42, 4 May 2008
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 Sun May 4 22:42:42 2008
