1O8U

The 2 Angstrom Structure of 6-Oxo Camphor Hydrolase: New Structural Diversity in the Crotonase Superfamily

Summary for 1O8U

• Entry DOI: 10.2210/pdb1o8u/pdb
• Descriptor: 6-OXO CAMPHOR HYDROLASE, SODIUM ION (3 entities in total)
• Functional Keywords: hydrolase, crotonase, terpene metabolism, rhodococcuse
• Biological source: RHODOCOCCUS ERYTHROPOLIS (ACTINOMYCETE)
• Total number of polymer chains: 6
• Total formula weight: 171125.41

Authors

Grogan, G.,Whittingham, J.L.,Turkenburg, J.P.,Verma, C.S.,Walsh, M.A. (deposition date: 2002-12-04, release date: 2003-01-24, Last modification date: 2024-05-08)

Primary citation

Whittingham, J.L.,Turkenburg, J.P.,Verma, C.S.,Walsh, M.A.,Grogan, G.
The 2 a Crystal Structure of 6-Oxo Camphor Hydrolase: New Structural Diversity in the Crotonase Superfamily
J.Biol.Chem., 278:1744-, 2003

PubMed Abstract: 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.

PubMed: 12421807
DOI: 10.1074/JBC.M211188200

Experimental method

X-RAY DIFFRACTION (2 Å)