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] |
| Copyright of Acta Crystallographica: Section F (Wiley-Blackwell) is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
| FullText | Text: Availability: 0 |
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| Header | DbId: egs DbLabel: Engineering Source An: 110812299 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: New structural insights and molecular-modelling studies of 4-methyl-5-β-hydroxyethylthiazole kinase from Pyrococcus horikoshii OT3 ( PhThiK). – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Jeyakanthan%2C+Jeyaraman%22">Jeyakanthan, Jeyaraman</searchLink><br /><searchLink fieldCode="AR" term="%22Thamotharan%2C+Subbiah%22">Thamotharan, Subbiah</searchLink><br /><searchLink fieldCode="AR" term="%22Velmurugan%2C+Devadasan%22">Velmurugan, Devadasan</searchLink><br /><searchLink fieldCode="AR" term="%22Rao%2C+Vaijayanthimala+Surya+Narayna%22">Rao, Vaijayanthimala Surya Narayna</searchLink><br /><searchLink fieldCode="AR" term="%22Nagarajan%2C+Shanthi%22">Nagarajan, Shanthi</searchLink><br /><searchLink fieldCode="AR" term="%22Shinkai%2C+Akeo%22">Shinkai, Akeo</searchLink><br /><searchLink fieldCode="AR" term="%22Kuramitsu%2C+Seiki%22">Kuramitsu, Seiki</searchLink><br /><searchLink fieldCode="AR" term="%22Yokoyama%2C+Shigeyuki%22">Yokoyama, Shigeyuki</searchLink> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Acta+Crystallographica%3A+Section+F+%28Wiley-Blackwell%29%22">Acta Crystallographica: Section F (Wiley-Blackwell)</searchLink>. Oct2009, Vol. 65 Issue 10, p978-986. 9p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Phosphorylation%22">Phosphorylation</searchLink><br /><searchLink fieldCode="DE" term="%22Pyrococcus+horikoshii%22">Pyrococcus horikoshii</searchLink><br /><searchLink fieldCode="DE" term="%22Hydroxyl+group%22">Hydroxyl group</searchLink><br /><searchLink fieldCode="DE" term="%22Nucleotides%22">Nucleotides</searchLink><br /><searchLink fieldCode="DE" term="%22Bacillus+subtilis%22">Bacillus subtilis</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: 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] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Acta Crystallographica: Section F (Wiley-Blackwell) is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1107/S1744309109036033 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 9 StartPage: 978 Subjects: – SubjectFull: Phosphorylation Type: general – SubjectFull: Pyrococcus horikoshii Type: general – SubjectFull: Hydroxyl group Type: general – SubjectFull: Nucleotides Type: general – SubjectFull: Bacillus subtilis Type: general Titles: – TitleFull: New structural insights and molecular-modelling studies of 4-methyl-5-β-hydroxyethylthiazole kinase from Pyrococcus horikoshii OT3 ( PhThiK). Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Jeyakanthan, Jeyaraman – PersonEntity: Name: NameFull: Thamotharan, Subbiah – PersonEntity: Name: NameFull: Velmurugan, Devadasan – PersonEntity: Name: NameFull: Rao, Vaijayanthimala Surya Narayna – PersonEntity: Name: NameFull: Nagarajan, Shanthi – PersonEntity: Name: NameFull: Shinkai, Akeo – PersonEntity: Name: NameFull: Kuramitsu, Seiki – PersonEntity: Name: NameFull: Yokoyama, Shigeyuki IsPartOfRelationships: – BibEntity: Dates: – D: 01 M: 10 Text: Oct2009 Type: published Y: 2009 Identifiers: – Type: issn-print Value: 17443091 Numbering: – Type: volume Value: 65 – Type: issue Value: 10 Titles: – TitleFull: Acta Crystallographica: Section F (Wiley-Blackwell) Type: main |
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