1o8u
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1o8u |SIZE=350|CAPTION= <scene name='initialview01'>1o8u</scene>, resolution 2.00Å | |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> | |SITE= <scene name='pdbsite=AC1:Na+Binding+Site+For+Chain+D'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=NA:SODIUM ION'>NA</scene> | + | |LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Walsh, M A.]] | [[Category: Walsh, M A.]] | ||
[[Category: Whittingham, J L.]] | [[Category: Whittingham, J L.]] | ||
| - | [[Category: NA]] | ||
[[Category: crotonase]] | [[Category: crotonase]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| Line 33: | Line 35: | ||
[[Category: terpene metabolism]] | [[Category: terpene metabolism]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:41:35 2008'' |
Revision as of 19:41, 30 March 2008
| |||||||
| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 Sun Mar 30 22:41:35 2008
