1on3
From Proteopedia
(New page: 200px<br /><applet load="1on3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1on3, resolution 1.90Å" /> '''Transcarboxylase 12S...) |
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| - | [[Image:1on3.jpg|left|200px]]<br /><applet load="1on3" size=" | + | [[Image:1on3.jpg|left|200px]]<br /><applet load="1on3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1on3, resolution 1.90Å" /> | caption="1on3, resolution 1.90Å" /> | ||
'''Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core (with methylmalonyl-coenzyme a and methylmalonic acid bound)'''<br /> | '''Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core (with methylmalonyl-coenzyme a and methylmalonic acid bound)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Transcarboxylase from Propionibacterium shermanii is a 1.2 MDa multienzyme | + | 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== | ==About this Structure== | ||
| - | 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 CD, MCA, DXX and MPD 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:// | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: Propionibacterium freudenreichii]] | [[Category: Propionibacterium freudenreichii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Carey, P | + | [[Category: Carey, P R.]] |
| - | [[Category: Hall, P | + | [[Category: Hall, P R.]] |
[[Category: Pustai-Carey, M.]] | [[Category: Pustai-Carey, M.]] | ||
| - | [[Category: Rivera-Hainaj, R | + | [[Category: Rivera-Hainaj, R E.]] |
| - | [[Category: Wang, Y | + | [[Category: Wang, Y F.]] |
| - | [[Category: Yee, V | + | [[Category: Yee, V C.]] |
[[Category: Zheng, X.]] | [[Category: Zheng, X.]] | ||
[[Category: CD]] | [[Category: CD]] | ||
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[[Category: transcarboxylase]] | [[Category: transcarboxylase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:19:34 2008'' |
Revision as of 12:19, 21 February 2008
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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)
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 with , , and as ligands. Active as Methylmalonyl-CoA carboxytransferase, with EC number 2.1.3.1 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 Feb 21 14:19:34 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 | DXX | MCA | MPD | Carboxyl transferase | Crystal structure | Domain duplication | Multienzyme complex | Transcarboxylase
