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New structural insights and molecular-modelling studies of 4-methyl-5-beta-hydroxyethylthiazole kinase from Pyrococcus horikoshii OT3 (PhThiK)

Jeyakanthan, Jeyaraman and Thamotharan, Subbiah and Velmurugan, Devadasan and Rao, Vaijayanthimala Surya Narayna and Nagarajan, Shanthi and Shinkai, Akeo and Kuramitsu, Seiki and Yokoyama, Shigeyuki (2009) New structural insights and molecular-modelling studies of 4-methyl-5-beta-hydroxyethylthiazole kinase from Pyrococcus horikoshii OT3 (PhThiK). In: Acta Crystallographica Section F Structural Biology and Crystallization Communications, 65 (Part 1). pp. 978-986.

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Official URL: http://scripts.iucr.org/cgi-bin/paper?S17443091090...

Abstract

4-Methyl-5-beta-hydroxyethylthiazole kinase (ThiK) catalyses the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole. This work reports the first crystal structure of an archaeal ThiK: that from Pyrococcus horikoshii OT3 (PhThiK) at 1.85 angstrom resolution with a phosphate ion occupying the position of the beta-phosphate of the nucleotide. The topology of this enzyme shows the typical ribokinase fold of an alpha/beta protein. The overall structure of PhThiK is similar to those of Bacillus subtilis ThiK (BsThiK) and Enterococcus faecalis V583 ThiK (EfThiK). Sequence analysis of ThiK enzymes from various sources indicated that three-quarters of the residues involved in interfacial regions are conserved. It also revealed that the amino-acid residues in the nucleotide-binding, magnesium ion-binding and substrate-binding sites are conserved. Binding of the nucleotide and substrate to the ThiK enzyme do not influence the quaternary association (trimer) as revealed by the crystal structure of PhThiK.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to John Wiley and Sons.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 07 Jan 2010 05:38
Last Modified: 19 Sep 2010 05:50
URI: http://eprints.iisc.ernet.in/id/eprint/24561

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