1on3

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[[Image:1on3.jpg|left|200px]]<br /><applet load="1on3" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1on3.jpg|left|200px]]
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caption="1on3, resolution 1.90&Aring;" />
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'''Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core (with methylmalonyl-coenzyme a and methylmalonic acid bound)'''<br />
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{{Structure
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|PDB= 1on3 |SIZE=350|CAPTION= <scene name='initialview01'>1on3</scene>, resolution 1.90&Aring;
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|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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|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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|GENE=
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}}
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'''Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core (with methylmalonyl-coenzyme a and methylmalonic acid bound)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1ON3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Propionibacterium_freudenreichii Propionibacterium freudenreichii] with <scene name='pdbligand=CD:'>CD</scene>, <scene name='pdbligand=MCA:'>MCA</scene>, <scene name='pdbligand=DXX:'>DXX</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ON3 OCA].
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1ON3 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=1ON3 OCA].
==Reference==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12743028 12743028]
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:19:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:13:04 2008''

Revision as of 11:13, 20 March 2008

Image:1on3.jpg


PDB ID 1on3

Drag the structure with the mouse to rotate
, resolution 1.90Å
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 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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