6req
From Proteopedia
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|PDB= 6req |SIZE=350|CAPTION= <scene name='initialview01'>6req</scene>, resolution 2.20Å | |PDB= 6req |SIZE=350|CAPTION= <scene name='initialview01'>6req</scene>, resolution 2.20Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=3CP:3-CARBOXYPROPYL-COENZYME+A'>3CP</scene>, <scene name='pdbligand=B12:COBALAMIN'>B12</scene> | + | |LIGAND= <scene name='pdbligand=3CP:3-CARBOXYPROPYL-COENZYME+A'>3CP</scene>, <scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|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]) | |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]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6req FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6req OCA], [http://www.ebi.ac.uk/pdbsum/6req PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=6req RCSB]</span> | ||
}} | }} | ||
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[[Category: Evans, P R.]] | [[Category: Evans, P R.]] | ||
[[Category: Mancia, F.]] | [[Category: Mancia, F.]] | ||
| - | [[Category: 3CP]] | ||
| - | [[Category: B12]] | ||
| - | [[Category: GOL]] | ||
[[Category: intramolecular transferase]] | [[Category: intramolecular transferase]] | ||
[[Category: isomerase]] | [[Category: isomerase]] | ||
[[Category: mutase]] | [[Category: mutase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:43:32 2008'' |
Revision as of 02:43, 31 March 2008
| |||||||
| , 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
