1rqh

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[[Image:1rqh.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_1rqh| PDB=1rqh | SCENE= }}
{{STRUCTURE_1rqh| PDB=1rqh | SCENE= }}
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'''Propionibacterium shermanii transcarboxylase 5S subunit bound to pyruvic acid'''
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===Propionibacterium shermanii transcarboxylase 5S subunit bound to pyruvic acid===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_15329673}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15329673 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15329673}}
==About this Structure==
==About this Structure==
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==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://www.ncbi.nlm.nih.gov/pubmed/15329673 15329673]
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]
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Expression and crystallization of several forms of the Propionibacterium shermanii transcarboxylase 5S subunit., Hall PR, Zheng R, Pusztai-Carey M, van den Akker F, Carey PR, Yee VC, Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):521-3. Epub 2004, Feb 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14993680 14993680]
[[Category: Methylmalonyl-CoA carboxytransferase]]
[[Category: Methylmalonyl-CoA carboxytransferase]]
[[Category: Propionibacterium freudenreichii subsp. shermanii]]
[[Category: Propionibacterium freudenreichii subsp. shermanii]]
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[[Category: Tim-barrel]]
[[Category: Tim-barrel]]
[[Category: Transcarboxylase]]
[[Category: Transcarboxylase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:47:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:32:41 2008''

Revision as of 12:32, 29 July 2008

Image:1rqh.png

Template:STRUCTURE 1rqh

Propionibacterium shermanii transcarboxylase 5S subunit bound to pyruvic acid

Template:ABSTRACT PUBMED 15329673

About this Structure

1RQH 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

Expression and crystallization of several forms of the Propionibacterium shermanii transcarboxylase 5S subunit., Hall PR, Zheng R, Pusztai-Carey M, van den Akker F, Carey PR, Yee VC, Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):521-3. Epub 2004, Feb 25. PMID:14993680

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