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1on9
From Proteopedia
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| - | [[Image:1on9.jpg|left|200px]] | + | [[Image:1on9.jpg|left|200px]] |
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| - | '''Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core (with hydrolyzed methylmalonyl-coenzyme a bound)''' | + | {{Structure |
| + | |PDB= 1on9 |SIZE=350|CAPTION= <scene name='initialview01'>1on9</scene>, resolution 2.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=MCA:METHYLMALONYL-COENZYME+A'>MCA</scene> and <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Methylmalonyl-CoA_carboxytransferase Methylmalonyl-CoA carboxytransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.1 2.1.3.1] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core (with hydrolyzed methylmalonyl-coenzyme a bound)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ON9 is a [ | + | 1ON9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Propionibacterium_freudenreichii Propionibacterium freudenreichii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ON9 OCA]. |
==Reference== | ==Reference== | ||
| - | Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core., Hall PR, Wang YF, Rivera-Hainaj RE, Zheng X, Pustai-Carey M, Carey PR, Yee VC, EMBO J. 2003 May 15;22(10):2334-47. PMID:[http:// | + | Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core., Hall PR, Wang YF, Rivera-Hainaj RE, Zheng X, Pustai-Carey M, Carey PR, Yee VC, EMBO J. 2003 May 15;22(10):2334-47. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12743028 12743028] |
[[Category: Methylmalonyl-CoA carboxytransferase]] | [[Category: Methylmalonyl-CoA carboxytransferase]] | ||
[[Category: Propionibacterium freudenreichii]] | [[Category: Propionibacterium freudenreichii]] | ||
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[[Category: transcarboxylase]] | [[Category: transcarboxylase]] | ||
| - | ''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 13:13:11 2008'' |
Revision as of 11:13, 20 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Activity: | Methylmalonyl-CoA carboxytransferase, with EC number 2.1.3.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core (with hydrolyzed methylmalonyl-coenzyme a bound)
Overview
Transcarboxylase from Propionibacterium shermanii is a 1.2 MDa multienzyme complex that couples two carboxylation reactions, transferring CO(2)(-) from methylmalonyl-CoA to pyruvate, yielding propionyl-CoA and oxaloacetate. The 1.9 A resolution crystal structure of the central 12S hexameric core, which catalyzes the first carboxylation reaction, has been solved bound to its substrate methylmalonyl-CoA. Overall, the structure reveals two stacked trimers related by 2-fold symmetry, and a domain duplication in the monomer. In the active site, the labile carboxylate group of methylmalonyl-CoA is stabilized by interaction with the N-termini of two alpha-helices. The 12S domains are structurally similar to the crotonase/isomerase superfamily, although only domain 1 of each 12S monomer binds ligand. The 12S reaction is similar to that of human propionyl-CoA carboxylase, whose beta-subunit has 50% sequence identity with 12S. A homology model of the propionyl-CoA carboxylase beta-subunit, based on this 12S crystal structure, provides new insight into the propionyl-CoA carboxylase mechanism, its oligomeric structure and the molecular basis of mutations responsible for enzyme deficiency in propionic acidemia.
About this Structure
1ON9 is a Single protein structure of sequence from Propionibacterium freudenreichii. Full crystallographic information is available from OCA.
Reference
Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core., Hall PR, Wang YF, Rivera-Hainaj RE, Zheng X, Pustai-Carey M, Carey PR, Yee VC, EMBO J. 2003 May 15;22(10):2334-47. PMID:12743028
Page seeded by OCA on Thu Mar 20 13:13:11 2008
Categories: Methylmalonyl-CoA carboxytransferase | Propionibacterium freudenreichii | Single protein | Carey, P R. | Hall, P R. | Pustai-Carey, M. | Rivera-Hainaj, R E. | Wang, Y F. | Yee, V C. | Zheng, X. | CD | MCA | MPD | Carboxyl transferase | Crystal structure | Domain duplication | Multienzyme complex | Transcarboxylase
