1o8u
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1o8u.jpg|left|200px]] | + | [[Image:1o8u.jpg|left|200px]] |
| - | + | ||
| - | '''THE 2 ANGSTROM STRUCTURE OF 6-OXO CAMPHOR HYDROLASE: NEW STRUCTURAL DIVERSITY IN THE CROTONASE SUPERFAMILY''' | + | {{Structure |
| + | |PDB= 1o8u |SIZE=350|CAPTION= <scene name='initialview01'>1o8u</scene>, resolution 2.00Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Na+Binding+Site+For+Chain+D'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=NA:SODIUM ION'>NA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THE 2 ANGSTROM STRUCTURE OF 6-OXO CAMPHOR HYDROLASE: NEW STRUCTURAL DIVERSITY IN THE CROTONASE SUPERFAMILY''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1O8U is a [ | + | 1O8U is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rhodococcus_erythropolis Rhodococcus erythropolis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O8U OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12421807 12421807] |
[[Category: Rhodococcus erythropolis]] | [[Category: Rhodococcus erythropolis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 24: | Line 33: | ||
[[Category: terpene metabolism]] | [[Category: terpene metabolism]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:07:22 2008'' |
Revision as of 11:07, 20 March 2008
| |||||||
| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 13:07:22 2008
