JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published In Press as doi:10.1074/jbc.M110787200 on December 19, 2001

J. Biol. Chem., Vol. 277, Issue 11, 9462-9467, March 15, 2002
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
277/11/9462    most recent
M110787200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Yang, D.
Right arrow Articles by Sacchettini, J. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yang, D.
Right arrow Articles by Sacchettini, J. C.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Structure of the Methanococcus jannaschii Mevalonate Kinase, a Member of the GHMP Kinase Superfamily*

Dong YangDagger , Lance W. Shipman§, Charles A. Roessner, A. Ian Scott, and James C. SacchettiniDagger ||

From the Dagger  Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843-2128 and  Department of Chemistry, Texas A&M University, College Station, Texas 77843-3255

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 from M. jannaschii. In addition, the enzyme shows structural similarity with mevalonate 5-diphosphate decarboxylase and domain IV of elongation factor G. The active site of MVK is in the cleft between its N- and C-terminal domains. Several structural motifs conserved among species, including a phosphate-binding loop, have been found in this cavity. Asp155, 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.

* Use of the Argonne National Laboratory Structural Biology Center beamlines at the Advanced Photon Source was supported by the Office of Energy Research, United States Department of Energy, under Contract W-31-109-ENG-38. This work was supported by the Robert A. Welch Foundation and by a grant from the National Institutes of Health.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The atomic coordinates and the structure factors (code 1KKH) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

§ Current address: Dept. of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322.

|| To whom correspondence should be addressed. Tel.: 979-862-7636; Fax: 979-862-7638; E-mail: sacchett@tamu.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 GeneticsHome page
C. Q. Diep, X. Tao, V. Pilauri, M. Losiewicz, T. E. Blank, and J. E. Hopper
Genetic Evidence for Sites of Interaction Between the Gal3 and Gal80 Proteins of the Saccharomyces cerevisiae GAL Gene Switch
Genetics, February 1, 2008; 178(2): 725 - 736.
[Abstract] [Full Text] [PDF]

Home page
 GeneticsHome page
C. Q. Diep, G. Peng, M. Bewley, V. Pilauri, I. Ropson, and J. E. Hopper
Intragenic Suppression of Gal3C Interaction With Gal80 in the Saccharomyces cerevisiae GAL Gene Switch
Genetics, January 1, 2006; 172(1): 77 - 87.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. B. Thoden, C. A. Sellick, D. J. Timson, R. J. Reece, and H. M. Holden
Molecular Structure of Saccharomyces cerevisiae Gal1p, a Bifunctional Galactokinase and Transcriptional Inducer
J. Biol. Chem., November 4, 2005; 280(44): 36905 - 36911.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. B. Thoden and H. M. Holden
The Molecular Architecture of Human N-Acetylgalactosamine Kinase
J. Biol. Chem., September 23, 2005; 280(38): 32784 - 32791.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
S. S. Doun, J. W. Burgner II, S. D. Briggs, and V. W. Rodwell
Enterococcus faecalis phosphomevalonate kinase
Protein Sci., May 1, 2005; 14(5): 1134 - 1139.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. B. Thoden, D. J. Timson, R. J. Reece, and H. M. Holden
Molecular Structure of Human Galactokinase: IMPLICATIONS FOR TYPE II GALACTOSEMIA
J. Biol. Chem., March 11, 2005; 280(10): 9662 - 9670.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. K. Nair and K. M. J. Menon
Isolation and Characterization of a Novel trans-Factor for Luteinizing Hormone Receptor mRNA from Ovary
J. Biol. Chem., April 9, 2004; 279(15): 14937 - 14944.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
M. Hedl and V. W. Rodwell
Enterococcus faecalis mevalonate kinase
Protein Sci., March 1, 2004; 13(3): 687 - 693.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
N. E. Voynova, S. E. Rios, and H. M. Miziorko
Staphylococcus aureus Mevalonate Kinase: Isolation and Characterization of an Enzyme of the Isoprenoid Biosynthetic Pathway
J. Bacteriol., January 1, 2004; 186(1): 61 - 67.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
H. M. Holden, I. Rayment, and J. B. Thoden
Structure and Function of Enzymes of the Leloir Pathway for Galactose Metabolism
J. Biol. Chem., November 7, 2003; 278(45): 43885 - 43888.
[Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. B. Thoden and H. M. Holden
Molecular Structure of Galactokinase
J. Biol. Chem., August 29, 2003; 278(35): 33305 - 33311.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. Wada, T. Kuzuyama, S. Satoh, S. Kuramitsu, S. Yokoyama, S. Unzai, J. R.H. Tame, and S.-Y. Park
Crystal Structure of 4-(Cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase, an Enzyme in the Non-mevalonate Pathway of Isoprenoid Synthesis
J. Biol. Chem., August 8, 2003; 278(32): 30022 - 30027.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
L. Miallau, M. S. Alphey, L. E. Kemp, G. A. Leonard, S. M. McSweeney, S. Hecht, A. Bacher, W. Eisenreich, F. Rohdich, and W. N. Hunter
Biosynthesis of isoprenoids: Crystal structure of 4-diphosphocytidyl-2C-methyl-D-erythritol kinase
PNAS, August 5, 2003; 100(16): 9173 - 9178.
[Abstract] [Full Text] [PDF]

Home page
 Genes Dev.Home page
J. G. Luz, C. A. Hassig, C. Pickle, A. Godzik, B. J. Meyer, and I. A. Wilson
XOL-1, primary determinant of sexual fate in C. elegans, is a GHMP kinase family member and a structural prototype for a class of developmental regulators
Genes & Dev., April 15, 2003; 17(8): 977 - 990.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
D. Pilloff, K. Dabovic, M. J. Romanowski, J. B. Bonanno, M. Doherty, S. K. Burley, and T. S. Leyh
The Kinetic Mechanism of Phosphomevalonate Kinase
J. Biol. Chem., February 7, 2003; 278(7): 4510 - 4515.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Z. Fu, M. Wang, D. Potter, H. M. Miziorko, and J.-J. P. Kim
The Structure of a Binary Complex between a Mammalian Mevalonate Kinase and ATP. INSIGHTS INTO THE REACTION MECHANISM AND HUMAN INHERITED DISEASE
J. Biol. Chem., May 10, 2002; 277(20): 18134 - 18142.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.