New structural insights and molecular-modelling studies of 4-methyl-5-β-hydroxyethylthiazole kinase from Pyrococcus horikoshii OT3 ( PhThiK).
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| Title: | New structural insights and molecular-modelling studies of 4-methyl-5-β-hydroxyethylthiazole kinase from Pyrococcus horikoshii OT3 ( PhThiK). |
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| Authors: | Jeyakanthan, Jeyaraman, Thamotharan, Subbiah, Velmurugan, Devadasan, Rao, Vaijayanthimala Surya Narayna, Nagarajan, Shanthi, Shinkai, Akeo, Kuramitsu, Seiki, Yokoyama, Shigeyuki |
| Source: | Acta Crystallographica: Section F (Wiley-Blackwell). Oct2009, Vol. 65 Issue 10, p978-986. 9p. |
| Subjects: | Phosphorylation, Pyrococcus horikoshii, Hydroxyl group, Nucleotides, Bacillus subtilis |
| Abstract: | 4-Methyl-5-β-hydroxyethylthiazole kinase (ThiK) catalyses the phosphorylation of the hydroxyl group of 4-methyl-5-β-hydroxyethylthiazole. This work reports the first crystal structure of an archaeal ThiK: that from Pyrococcus horikoshii OT3 ( PhThiK) at 1.85 Å resolution with a phosphate ion occupying the position of the β-phosphate of the nucleotide. The topology of this enzyme shows the typical ribokinase fold of an α/β 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. [ABSTRACT FROM AUTHOR] |
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| Database: | Engineering Source |
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