Preliminary X-ray crystallographic analysis of biotin carboxylase isolated from Escherichia coli.
Acetyl CoA carboxylase catalyzes the first committed step in the biosynthesis of long chain fatty acids. In Escherichia coli, the enzyme consists of three subunits that are isolated separately and display distinct functional properties. Here we report the crystallization and preliminary X-ray analysis of one of these components, namely biotin carboxylase. The crystals are grown by microdialysis against 10 mM potassium phosphate (pH 7.0), 1 mM EDTA, 2 mM DTT and 1 mM NaN3 at 4 degrees C. They belong to the space group P2(1)2(1)2(1) with unit cell dimensions of a = 61.9 A, b = 96.1 A and c = 180.6 A and contain one dimer per asymmetric unit. The crystals diffract to a nominal resolution of 2.2 A. From a mechanistic standpoint, biotin carboxylase is especially interesting in that it is the smallest protein within its class and is one of only two carboxylases that can utilize free biotin as a substrate.[1]References
- Preliminary X-ray crystallographic analysis of biotin carboxylase isolated from Escherichia coli. Waldrop, G., Holden, H.M., Rayment, I. J. Mol. Biol. (1994) [Pubmed]
Annotations and hyperlinks in this abstract are from individual authors of WikiGenes or automatically generated by the WikiGenes Data Mining Engine. The abstract is from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenesOpen Access LicencePrivacy PolicyTerms of Useapsburg
