1on3

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|PDB= 1on3 |SIZE=350|CAPTION= <scene name='initialview01'>1on3</scene>, resolution 1.90&Aring;
|PDB= 1on3 |SIZE=350|CAPTION= <scene name='initialview01'>1on3</scene>, resolution 1.90&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=MCA:METHYLMALONYL-COENZYME+A'>MCA</scene>, <scene name='pdbligand=DXX:METHYLMALONIC+ACID'>DXX</scene> and <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>
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|LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=DXX:METHYLMALONIC+ACID'>DXX</scene>, <scene name='pdbligand=MCA:METHYLMALONYL-COENZYME+A'>MCA</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>
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|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]
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|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=[[1on9|1on9]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1on3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1on3 OCA], [http://www.ebi.ac.uk/pdbsum/1on3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1on3 RCSB]</span>
}}
}}
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[[Category: Yee, V C.]]
[[Category: Yee, V C.]]
[[Category: Zheng, X.]]
[[Category: Zheng, X.]]
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[[Category: CD]]
 
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[[Category: DXX]]
 
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[[Category: MCA]]
 
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[[Category: MPD]]
 
[[Category: carboxyl transferase]]
[[Category: carboxyl transferase]]
[[Category: crystal structure]]
[[Category: crystal structure]]
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[[Category: transcarboxylase]]
[[Category: transcarboxylase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:13:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:47:36 2008''

Revision as of 19:47, 30 March 2008


PDB ID 1on3

Drag the structure with the mouse to rotate
, resolution 1.90Å
Ligands: , , ,
Activity: Methylmalonyl-CoA carboxytransferase, with EC number 2.1.3.1
Related: 1on9


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core (with methylmalonyl-coenzyme a and methylmalonic acid 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

1ON3 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

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