1rr2: Difference between revisions
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[[Image:1rr2.gif|left|200px]] | [[Image:1rr2.gif|left|200px]] | ||
'''Propionibacterium shermanii transcarboxylase 5S subunit bound to 2-ketobutyric acid''' | {{Structure | ||
|PDB= 1rr2 |SIZE=350|CAPTION= <scene name='initialview01'>1rr2</scene>, resolution 2.00Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene> and <scene name='pdbligand=2KT:2-KETOBUTYRIC ACID'>2KT</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= 5S ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1752 Propionibacterium freudenreichii subsp. shermanii]) | |||
}} | |||
'''Propionibacterium shermanii transcarboxylase 5S subunit bound to 2-ketobutyric acid''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1RR2 is a [ | 1RR2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RR2 OCA]. | ||
==Reference== | ==Reference== | ||
Transcarboxylase 5S structures: assembly and catalytic mechanism of a multienzyme complex subunit., Hall PR, Zheng R, Antony L, Pusztai-Carey M, Carey PR, Yee VC, EMBO J. 2004 Sep 15;23(18):3621-31. Epub 2004 Aug 26. PMID:[http:// | Transcarboxylase 5S structures: assembly and catalytic mechanism of a multienzyme complex subunit., Hall PR, Zheng R, Antony L, Pusztai-Carey M, Carey PR, Yee VC, EMBO J. 2004 Sep 15;23(18):3621-31. Epub 2004 Aug 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15329673 15329673] | ||
[[Category: Methylmalonyl-CoA carboxytransferase]] | [[Category: Methylmalonyl-CoA carboxytransferase]] | ||
[[Category: Propionibacterium freudenreichii subsp. shermanii]] | [[Category: Propionibacterium freudenreichii subsp. shermanii]] | ||
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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 13:55:14 2008'' | ||
Revision as of 14:55, 20 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | 5S (Propionibacterium freudenreichii subsp. shermanii) | ||||||
| Activity: | Methylmalonyl-CoA carboxytransferase, with EC number 2.1.3.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Propionibacterium shermanii transcarboxylase 5S subunit bound to 2-ketobutyric acid
OverviewOverview
Transcarboxylase is a 1.2 million Dalton (Da) multienzyme complex from Propionibacterium shermanii that couples two carboxylation reactions, transferring CO(2)(-) from methylmalonyl-CoA to pyruvate to yield propionyl-CoA and oxaloacetate. Crystal structures of the 5S metalloenzyme subunit, which catalyzes the second carboxylation reaction, have been solved in free form and bound to its substrate pyruvate, product oxaloacetate, or inhibitor 2-ketobutyrate. The structure reveals a dimer of beta(8)alpha(8) barrels with an active site cobalt ion coordinated by a carbamylated lysine, except in the oxaloacetate complex in which the product's carboxylate group serves as a ligand instead. 5S and human pyruvate carboxylase (PC), an enzyme crucial to gluconeogenesis, catalyze similar reactions. A 5S-based homology model of the PC carboxyltransferase domain indicates a conserved mechanism and explains the molecular basis of mutations in lactic acidemia. PC disease mutations reproduced in 5S result in a similar decrease in carboxyltransferase activity and crystal structures with altered active sites.
About this StructureAbout this Structure
1RR2 is a Single protein structure of sequence from Propionibacterium freudenreichii subsp. shermanii. Full crystallographic information is available from OCA.
ReferenceReference
Transcarboxylase 5S structures: assembly and catalytic mechanism of a multienzyme complex subunit., Hall PR, Zheng R, Antony L, Pusztai-Carey M, Carey PR, Yee VC, EMBO J. 2004 Sep 15;23(18):3621-31. Epub 2004 Aug 26. PMID:15329673
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