1o8u
From Proteopedia
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THE 2 ANGSTROM STRUCTURE OF 6-OXO CAMPHOR HYDROLASE: NEW STRUCTURAL DIVERSITY IN THE CROTONASE SUPERFAMILY
Overview
6-Oxo camphor hydrolase (OCH) is an enzyme of the crotonase superfamily, that catalyzes carbon-carbon bond cleavage in bicyclic beta-diketones via, a retro-Claisen reaction (Grogan, G., Roberts, G. A., Bougioukou, D., Turner, N. J., and Flitsch, S. L. (2001) J. Biol. Chem. 276, 12565-12572)., The native structure of OCH has been solved at 2.0-A resolution with, selenomethionine multiple wave anomalous dispersion and refined to a final, R(free) of 19.0. The structure of OCH consists of a dimer of trimers that, resembles the "parent" enzyme of the superfamily, enoyl-CoA hydratase. In, contrast to enoyl-CoA hydratase, however, two octahedrally coordinated, sodium atoms are found at the 3-fold axis of the hexamer of OCH, and the, C-terminal helix of OCH does not form a discrete domain. Models ... [(full description)]
About this Structure
1O8U is a [Single protein] structure of sequence from [Rhodococcus erythropolis] with NA as [ligand]. Full crystallographic information is available from [OCA].
Reference
The 2-A crystal structure of 6-oxo camphor hydrolase. New structural diversity in the crotonase superfamily., Whittingham JL, Turkenburg JP, Verma CS, Walsh MA, Grogan G, J Biol Chem. 2003 Jan 17;278(3):1744-50. Epub 2002 Nov 5. PMID:12421807
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