Abstract |
The crystal structure of shikimate kinase from Mycobacterium tuberculosis (MtSK) complexed with MgADP and shikimic acid ( shikimate) has been determined at 2.3A resolution, clearly revealing the amino acid residues involved in shikimate binding. In MtSK, the Glu61 strictly conserved in SK forms a hydrogen bond and salt-bridge with Arg58 and assists in positioning the guanidinium group of Arg58 for shikimate binding. The carboxyl group of shikimate interacts with Arg58, Gly81, and Arg136, and hydroxyl groups with Asp34 and Gly80. The crystal structure of MtSK- MgADP- shikimate will provide crucial information for elucidation of the mechanism of SK-catalyzed reaction and for the development of a new generation of drugs against tuberculosis.
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Authors | José Henrique Pereira, Jaim Simões de Oliveira, Fernanda Canduri, Marcio Vinicius Bertacine Dias, Mário Sérgio Palma, Luiz Augusto Basso, Walter Filgueira de Azevedo Jr, Diógenes Santiago Santos |
Journal | Biochemical and biophysical research communications
(Biochem Biophys Res Commun)
Vol. 325
Issue 1
Pg. 10-7
(Dec 03 2004)
ISSN: 0006-291X [Print] United States |
PMID | 15522194
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Retracted Publication)
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Chemical References |
- Bacterial Proteins
- Shikimic Acid
- Adenosine Diphosphate
- Phosphotransferases (Alcohol Group Acceptor)
- shikimate kinase
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Topics |
- Adenosine Diphosphate
(chemistry)
- Bacterial Proteins
(chemistry, metabolism)
- Crystallography, X-Ray
- Hydrogen Bonding
- Models, Molecular
- Molecular Sequence Data
- Molecular Structure
- Mycobacterium tuberculosis
(chemistry, enzymology)
- Phosphotransferases (Alcohol Group Acceptor)
(chemistry, metabolism)
- Protein Binding
- Protein Structure, Tertiary
- Shikimic Acid
(chemistry, metabolism)
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