2gpw

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[[Image:2gpw.gif|left|200px]]
[[Image:2gpw.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2gpw |SIZE=350|CAPTION= <scene name='initialview01'>2gpw</scene>, resolution 2.20&Aring;
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The line below this paragraph, containing "STRUCTURE_2gpw", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Biotin_carboxylase Biotin carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.14 6.3.4.14] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= accC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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{{STRUCTURE_2gpw| PDB=2gpw | SCENE= }}
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|RELATEDENTRY=[[1w93|1W93]], [[1w96|1W96]], [[1dv1|1DV1]], [[1dv2|1DV2]], [[1bnc|1BNC]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gpw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gpw OCA], [http://www.ebi.ac.uk/pdbsum/2gpw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2gpw RCSB]</span>
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}}
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'''Crystal Structure of the Biotin Carboxylase Subunit, F363A Mutant, of Acetyl-CoA Carboxylase from Escherichia coli.'''
'''Crystal Structure of the Biotin Carboxylase Subunit, F363A Mutant, of Acetyl-CoA Carboxylase from Escherichia coli.'''
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[[Category: Shen, Y.]]
[[Category: Shen, Y.]]
[[Category: Tong, L.]]
[[Category: Tong, L.]]
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[[Category: atp-grasp]]
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[[Category: Atp-grasp]]
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[[Category: biotin-dependent]]
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[[Category: Biotin-dependent]]
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[[Category: carboxylase]]
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[[Category: Carboxylase]]
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[[Category: dimer-interface mutant]]
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[[Category: Dimer-interface mutant]]
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[[Category: fatty acid synthesis]]
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[[Category: Fatty acid synthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:23:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:19:53 2008''
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Revision as of 02:23, 4 May 2008

Template:STRUCTURE 2gpw

Crystal Structure of the Biotin Carboxylase Subunit, F363A Mutant, of Acetyl-CoA Carboxylase from Escherichia coli.


Overview

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.

About this Structure

2GPW 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 Page seeded by OCA on Sun May 4 05:23:03 2008

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