1rr2
From Proteopedia
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|PDB= 1rr2 |SIZE=350|CAPTION= <scene name='initialview01'>1rr2</scene>, resolution 2.00Å | |PDB= 1rr2 |SIZE=350|CAPTION= <scene name='initialview01'>1rr2</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene> | + | |LIGAND= <scene name='pdbligand=2KT:2-KETOBUTYRIC+ACID'>2KT</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</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] | + | |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= 5S ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1752 Propionibacterium freudenreichii subsp. shermanii]) | |GENE= 5S ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1752 Propionibacterium freudenreichii subsp. shermanii]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1rqb|1RQB]], [[1rqe|1RQE]], [[1rqh|1RQH]], [[1s3h|1S3H]], [[1s27|1S27]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rr2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rr2 OCA], [http://www.ebi.ac.uk/pdbsum/1rr2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rr2 RCSB]</span> | ||
}} | }} | ||
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[[Category: Yee, V C.]] | [[Category: Yee, V C.]] | ||
[[Category: Zheng, R.]] | [[Category: Zheng, R.]] | ||
| - | [[Category: 2KT]] | ||
| - | [[Category: CO]] | ||
[[Category: 2-ketobutyric acid]] | [[Category: 2-ketobutyric acid]] | ||
[[Category: carbamylated lysine]] | [[Category: carbamylated lysine]] | ||
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[[Category: transcarboxylase]] | [[Category: transcarboxylase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:31:49 2008'' |
Revision as of 20:31, 30 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | 5S (Propionibacterium freudenreichii subsp. shermanii) | ||||||
| Activity: | Methylmalonyl-CoA carboxytransferase, with EC number 2.1.3.1 | ||||||
| Related: | 1RQB, 1RQE, 1RQH, 1S3H, 1S27
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Propionibacterium shermanii transcarboxylase 5S subunit bound to 2-ketobutyric acid
Overview
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 Structure
1RR2 is a Single protein structure of sequence from Propionibacterium freudenreichii subsp. shermanii. Full crystallographic information is available from OCA.
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:15329673
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