2gpw
From Proteopedia
| Line 5: | Line 5: | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
| - | |ACTIVITY= [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] | + | |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> |
|GENE= accC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= accC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1w93|1W93]], [[1w96|1W96]], [[1dv1|1DV1]], [[1dv2|1DV2]], [[1bnc|1BNC]] | ||
| + | |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> | ||
}} | }} | ||
| Line 33: | Line 36: | ||
[[Category: fatty acid synthesis]] | [[Category: fatty acid synthesis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:19:53 2008'' |
Revision as of 00:19, 31 March 2008
| |||||||
| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | accC (Escherichia coli) | ||||||
| Activity: | Biotin carboxylase, with EC number 6.3.4.14 | ||||||
| Related: | 1W93, 1W96, 1DV1, 1DV2, 1BNC
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Mon Mar 31 03:19:53 2008
