1iuh: Difference between revisions
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'''Crystal structure of TT0787 of thermus thermophilus HB8''' | '''Crystal structure of TT0787 of thermus thermophilus HB8''' | ||
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[[Category: Shirouzu, M.]] | [[Category: Shirouzu, M.]] | ||
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
[[Category: | [[Category: Ligase]] | ||
[[Category: | [[Category: Riken structural genomics/proteomics initiative]] | ||
[[Category: | [[Category: Rsgi]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: | [[Category: Thermus thermophilus]] | ||
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Revision as of 20:25, 2 May 2008
Crystal structure of TT0787 of thermus thermophilus HB8
OverviewOverview
The 2'-5' RNA ligase family members are bacterial and archaeal RNA ligases that ligate 5' and 3' half-tRNA molecules with 2',3'-cyclic phosphate and 5'-hydroxyl termini, respectively, to the product containing the 2'-5' phosphodiester linkage. Here, the crystal structure of the 2'-5' RNA ligase protein from an extreme thermophile, Thermus thermophilus HB8, was solved at 2.5A resolution. The structure of the 2'-5' RNA ligase superimposes well on that of the Arabidopsis thaliana cyclic phosphodiesterase (CPDase), which hydrolyzes ADP-ribose 1",2"-cyclic phosphate (a product of the tRNA splicing reaction) to the monoester ADP-ribose 1"-phosphate. Although the sequence identity between the two proteins is remarkably low (9.3%), the 2'-5' RNA ligase and CPDase structures have two HX(T/S)X motifs in their corresponding positions. The HX(T/S)X motifs play important roles in the CPDase activity, and are conserved in both the CPDases and 2'-5' RNA ligases. Therefore, the catalytic mechanism of the 2'-5' RNA ligase may be similar to that of the CPDase. On the other hand, the electrostatic potential of the cavity of the 2'-5' RNA ligase is positive, but that of the CPDase is negative. Furthermore, in the CPDase, two loops with low B-factors cover the cavity. In contrast, in the 2'-5' RNA ligase, the corresponding loops form an open conformation and are flexible. These characteristics may be due to the differences in the substrates, tRNA and ADP-ribose 1",2"-cyclic phosphate.
About this StructureAbout this Structure
1IUH is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the 2'-5' RNA ligase from Thermus thermophilus HB8., Kato M, Shirouzu M, Terada T, Yamaguchi H, Murayama K, Sakai H, Kuramitsu S, Yokoyama S, J Mol Biol. 2003 Jun 20;329(5):903-11. PMID:12798681 Page seeded by OCA on Fri May 2 20:25:57 2008