The 2-A crystal structure of 6-oxo camphor hydrolase - New structural diversity in the crotonase superfamily

J L  Whittingham; J P  Turkenburg; C S  Verma; M A  Walsh; G  Grogan

doi:10.1074/jbc.M211188200

The 2-A crystal structure of 6-oxo camphor hydrolase - New structural diversity in the crotonase superfamily

J L Whittingham, J P Turkenburg, C S Verma, M A Walsh, G Grogan

Chemistry

Research output: Contribution to journal › Article › peer-review

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-Angstrom 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.

Original language	English
Pages (from-to)	1744-1750
Number of pages	7
Journal	Journal of Biological Chemistry
Volume	278
Issue number	3
DOIs	https://doi.org/10.1074/jbc.M211188200
Publication status	Published - 17 Jan 2003

Keywords

ENOYL-COA HYDRATASE
ANGSTROM RESOLUTION
PROTEIN
MOLSCRIPT
DYNAMICS
CATALYZE
PROGRAM
REVEALS
ENERGY

Access to Document

10.1074/jbc.M211188200

http://dx.doi.org/10.1074/jbc.M211188200

Cite this

@article{558976b248b84e858ca8cbe8e4d9c1e4,

title = "The 2-A crystal structure of 6-oxo camphor hydrolase - New structural diversity in the crotonase superfamily",

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-Angstrom 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.",

keywords = "ENOYL-COA HYDRATASE, ANGSTROM RESOLUTION, PROTEIN, MOLSCRIPT, DYNAMICS, CATALYZE, PROGRAM, REVEALS, ENERGY",

author = "Whittingham, {J L} and Turkenburg, {J P} and Verma, {C S} and Walsh, {M A} and G Grogan",

year = "2003",

month = jan,

day = "17",

doi = "10.1074/jbc.M211188200",

language = "English",

volume = "278",

pages = "1744--1750",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

number = "3",

}

TY - JOUR

T1 - The 2-A crystal structure of 6-oxo camphor hydrolase - New structural diversity in the crotonase superfamily

AU - Whittingham, J L

AU - Turkenburg, J P

AU - Verma, C S

AU - Walsh, M A

AU - Grogan, G

PY - 2003/1/17

Y1 - 2003/1/17

N2 - 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-Angstrom 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.

AB - 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-Angstrom 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.

KW - ENOYL-COA HYDRATASE

KW - ANGSTROM RESOLUTION

KW - PROTEIN

KW - MOLSCRIPT

KW - DYNAMICS

KW - CATALYZE

KW - PROGRAM

KW - REVEALS

KW - ENERGY

U2 - 10.1074/jbc.M211188200

DO - 10.1074/jbc.M211188200

M3 - Article

SN - 0021-9258

VL - 278

SP - 1744

EP - 1750

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 3

ER -