1o8u
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1o8u.jpg|left|200px]]<br /><applet load="1o8u" size=" | + | [[Image:1o8u.jpg|left|200px]]<br /><applet load="1o8u" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1o8u, resolution 2.00Å" /> | caption="1o8u, resolution 2.00Å" /> | ||
'''THE 2 ANGSTROM STRUCTURE OF 6-OXO CAMPHOR HYDROLASE: NEW STRUCTURAL DIVERSITY IN THE CROTONASE SUPERFAMILY'''<br /> | '''THE 2 ANGSTROM STRUCTURE OF 6-OXO CAMPHOR HYDROLASE: NEW STRUCTURAL DIVERSITY IN THE CROTONASE SUPERFAMILY'''<br /> | ||
| Line 7: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1O8U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodococcus_erythropolis Rhodococcus erythropolis] with NA as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Na Binding Site For Chain D'>AC1</scene>. Full crystallographic information is available from [http:// | + | 1O8U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodococcus_erythropolis Rhodococcus erythropolis] with <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Na+Binding+Site+For+Chain+D'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O8U OCA]. |
==Reference== | ==Reference== | ||
| Line 24: | Line 24: | ||
[[Category: terpene metabolism]] | [[Category: terpene metabolism]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:54:59 2008'' |
Revision as of 07:54, 3 February 2008
|
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 with as ligand. Known structural/functional Site: . 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 Sun Feb 3 09:54:59 2008
