We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1iuh

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1iuh.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1iuh.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1iuh| PDB=1iuh | SCENE= }}
{{STRUCTURE_1iuh| PDB=1iuh | SCENE= }}
-
'''Crystal structure of TT0787 of thermus thermophilus HB8'''
+
===Crystal structure of TT0787 of thermus thermophilus HB8===
-
==Overview==
+
<!--
-
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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12798681}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12798681 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12798681}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:25:57 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 14:01:17 2008''

Revision as of 11:01, 1 July 2008

Image:1iuh.png

Template:STRUCTURE 1iuh

Crystal structure of TT0787 of thermus thermophilus HB8

Template:ABSTRACT PUBMED 12798681

About this Structure

1IUH is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

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 Tue Jul 1 14:01:17 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1iuh"
Personal tools