1o8u

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[[Image:1o8u.jpg|left|200px]]
[[Image:1o8u.jpg|left|200px]]
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{{Structure
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|PDB= 1o8u |SIZE=350|CAPTION= <scene name='initialview01'>1o8u</scene>, resolution 2.00&Aring;
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The line below this paragraph, containing "STRUCTURE_1o8u", creates the "Structure Box" on the page.
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{{STRUCTURE_1o8u| PDB=1o8u | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o8u OCA], [http://www.ebi.ac.uk/pdbsum/1o8u PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1o8u RCSB]</span>
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'''THE 2 ANGSTROM STRUCTURE OF 6-OXO CAMPHOR HYDROLASE: NEW STRUCTURAL DIVERSITY IN THE CROTONASE SUPERFAMILY'''
'''THE 2 ANGSTROM STRUCTURE OF 6-OXO CAMPHOR HYDROLASE: NEW STRUCTURAL DIVERSITY IN THE CROTONASE SUPERFAMILY'''
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[[Category: Walsh, M A.]]
[[Category: Walsh, M A.]]
[[Category: Whittingham, J L.]]
[[Category: Whittingham, J L.]]
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[[Category: crotonase]]
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[[Category: Crotonase]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: rhodococcuse]]
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[[Category: Rhodococcuse]]
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[[Category: terpene metabolism]]
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[[Category: Terpene metabolism]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:31:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:41:35 2008''
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Revision as of 00:31, 3 May 2008

Image:1o8u.jpg

Template:STRUCTURE 1o8u

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 of the substrate, 6-oxo camphor, and a proposed enolate intermediate in the putative active site suggest possible mechanistic roles for Glu-244, Asp-154, His-122, His-45, and His-145.

About this Structure

1O8U is a Single protein structure of sequence from Rhodococcus erythropolis. 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 Page seeded by OCA on Sat May 3 03:31:54 2008

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