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Papers In Press, published online ahead of print December 19, 2001
J. Biol. Chem, 10.1074/jbc.M110787200
Submitted on November 9, 2001
Revised on December 18, 2001
Accepted on December 19, 2001

Structure of the methanococcus jannaschii mevalonate kinase - a member of the GHMP kinase superfamily

Dong Yang, Lance W. Shipman, Charles A. Roessner, A I. Scott, and James C. Sacchettini

Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843-2128

Corresponding Author: sacchett{at}tamu.edu

The mevalonate-dependent pathway is used by many organisms to synthesize isopentenyl pyrophosphate, the building block for the biosynthesis of many biologically important compounds, including farnesyl pyrophosphate, dolichol and many sterols. Mevalonate kinase (MVK) catalyzes a critical phosphoryl transfer step, producing mevalonate 5'-phosphate. The crystal structure of thermostable MVK from Methanococcus jannaschii has been determined at 2.4 Å, revealing an overall fold similar to the homoserine kinase (HSK) from Methanococcus jannaschii. In addition, the enzyme shows structural similarity with mevalonate 5-diphosphate decarboxylase (MDD) and the domain IV of elongation factor G. The active site of MVK is in the cleft between its N-terminal and C-terminal domains. Several structural motifs conserved among species, including a phosphate-binding loop, have been found in this cavity. Asp 155, an invariant residue among MVK sequences, is located close to the putative phosphate-binding site and has been assumed to play the catalytic role. Analysis of the MVK model, in the context of the other members of the GHMP kinase family offers the opportunity to understand both the mechanism of these enzymes and the structural details that may lead to the design of novel drugs.


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