1req
From Proteopedia
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|PDB= 1req |SIZE=350|CAPTION= <scene name='initialview01'>1req</scene>, resolution 2.0Å | |PDB= 1req |SIZE=350|CAPTION= <scene name='initialview01'>1req</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=DCA:DESULFO-COENZYME+A'>DCA</scene> | + | |LIGAND= <scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=DCA:DESULFO-COENZYME+A'>DCA</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= MUTA MUTB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1752 Propionibacterium freudenreichii subsp. shermanii]) | |GENE= MUTA MUTB ([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=1req FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1req OCA], [http://www.ebi.ac.uk/pdbsum/1req PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1req RCSB]</span> | ||
}} | }} | ||
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[[Category: Evans, P R.]] | [[Category: Evans, P R.]] | ||
[[Category: Mancia, F.]] | [[Category: Mancia, F.]] | ||
| - | [[Category: B12]] | ||
| - | [[Category: DCA]] | ||
| - | [[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 Sun Mar 30 23:27:06 2008'' |
Revision as of 20:27, 30 March 2008
| |||||||
| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | MUTA MUTB (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
Overview
BACKGROUND. The enzyme methylmalonyl-coenzyme A (CoA) mutase, an alphabeta heterodimer of 150 kDa, is a member of a class of enzymes that uses coenzyme B12 (adenosylcobalamin) as a cofactor. The enzyme induces the formation of an adenosyl radical from the cofactor. This radical then initiates a free-radical rearrangement of its substrate, succinyl-CoA, to methylmalonyl-CoA. RESULTS. Reported here is the crystal structure at 2 A resolution of methylmalonyl-CoA mutase from Propionibacterium shermanii in complex with coenzyme B12 and with the partial substrate desulpho-CoA (lacking the succinyl group and the sulphur atom of the substrate). The coenzyme is bound by a domain which shares a similar fold to those of flavodoxin and the B12-binding domain of methylcobalamin-dependent methionine synthase. The cobalt atom is coordinated, via a long bond, to a histidine from the protein. The partial substrate is bound along the axis of a (beta/alpha)8 TIM barrel domain. CONCLUSIONS. The histidine-cobalt distance is very long (2.5 A compared with 1.95-2.2 A in free cobalamins), suggesting that the enzyme positions the histidine in order to weaken the metal-carbon bond of the cofactor and favour the formation of the initial radical species. The active site is deeply buried, and the only access to it is through a narrow tunnel along the axis of the TIM barrel domain.
About this Structure
1REQ is a Protein complex structure of sequences from Propionibacterium freudenreichii subsp. shermanii. Full crystallographic information is available from OCA.
Reference
How coenzyme B12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2 A resolution., Mancia F, Keep NH, Nakagawa A, Leadlay PF, McSweeney S, Rasmussen B, Bosecke P, Diat O, Evans PR, Structure. 1996 Mar 15;4(3):339-50. PMID:8805541
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