6req
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:6req.gif|left|200px]] | + | [[Image:6req.gif|left|200px]] |
| - | + | ||
| - | '''METHYLMALONYL-COA MUTASE, 3-CARBOXYPROPYL-COA INHIBITOR COMPLEX''' | + | {{Structure |
| + | |PDB= 6req |SIZE=350|CAPTION= <scene name='initialview01'>6req</scene>, resolution 2.20Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=3CP:3-CARBOXYPROPYL-COENZYME+A'>3CP</scene>, <scene name='pdbligand=B12:COBALAMIN'>B12</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Methylmalonyl-CoA_mutase Methylmalonyl-CoA mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.2 5.4.99.2] | ||
| + | |GENE= MUTB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1752 Propionibacterium freudenreichii subsp. shermanii]), MUTA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1752 Propionibacterium freudenreichii subsp. shermanii]) | ||
| + | }} | ||
| + | |||
| + | '''METHYLMALONYL-COA MUTASE, 3-CARBOXYPROPYL-COA INHIBITOR COMPLEX''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 6REQ is a [ | + | 6REQ is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6REQ OCA]. |
==Reference== | ==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:[http:// | + | Crystal structure of substrate complexes of methylmalonyl-CoA mutase., Mancia F, Smith GA, Evans PR, Biochemistry. 1999 Jun 22;38(25):7999-8005. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10387043 10387043] |
[[Category: Methylmalonyl-CoA mutase]] | [[Category: Methylmalonyl-CoA mutase]] | ||
[[Category: Propionibacterium freudenreichii subsp. shermanii]] | [[Category: Propionibacterium freudenreichii subsp. shermanii]] | ||
| Line 23: | Line 32: | ||
[[Category: mutase]] | [[Category: mutase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:13:59 2008'' |
Revision as of 17:14, 20 March 2008
| |||||||
| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Gene: | MUTB (Propionibacterium freudenreichii subsp. shermanii), MUTA (Propionibacterium freudenreichii subsp. shermanii) | ||||||
| Activity: | Methylmalonyl-CoA mutase, with EC number 5.4.99.2 | ||||||
| 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 Thu Mar 20 19:13:59 2008
