2gps

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{{STRUCTURE_2gps| PDB=2gps | SCENE= }}
{{STRUCTURE_2gps| PDB=2gps | SCENE= }}
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'''Crystal Structure of the Biotin Carboxylase Subunit, E23R mutant, of Acetyl-CoA Carboxylase from Escherichia coli.'''
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===Crystal Structure of the Biotin Carboxylase Subunit, E23R mutant, of Acetyl-CoA Carboxylase from Escherichia coli.===
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==Overview==
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Acetyl-coenzyme A carboxylases (ACCs) have crucial roles in fatty acid metabolism. The biotin carboxylase (BC) subunit of Escherichia coli ACC is believed to be active only as a dimer, although the crystal structure shows that the active site of each monomer is 25 A from the dimer interface. We report here biochemical, biophysical, and structural characterizations of BC carrying single-site mutations in the dimer interface. Our studies demonstrate that two of the mutants, R19E and E23R, are monomeric in solution but have only a 3-fold loss in catalytic activity. The crystal structures of the E23R and F363A mutants show that they can still form the correct dimer at high concentrations. Our data suggest that dimerization is not an absolute requirement for the catalytic activity of the E. coli BC subunit, and we propose a new model for the molecular mechanism of action for BC in multisubunit and multidomain ACCs.
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{{ABSTRACT_PUBMED_16793549}}
==About this Structure==
==About this Structure==
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[[Category: Dimer-interface mutant]]
[[Category: Dimer-interface mutant]]
[[Category: Fatty acid synthesis]]
[[Category: Fatty acid synthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:22:52 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:05:55 2008''

Revision as of 11:05, 27 July 2008

Image:2gps.png

Template:STRUCTURE 2gps

Crystal Structure of the Biotin Carboxylase Subunit, E23R mutant, of Acetyl-CoA Carboxylase from Escherichia coli.

Template:ABSTRACT PUBMED 16793549

About this Structure

2GPS is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Is dimerization required for the catalytic activity of bacterial biotin carboxylase?, Shen Y, Chou CY, Chang GG, Tong L, Mol Cell. 2006 Jun 23;22(6):807-18. PMID:16793549

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