This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2mhi

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "2mhi" [edit=sysop:move=sysop])
Current revision (06:05, 15 May 2024) (edit) (undo)
 
(8 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 2mhi is ON HOLD
+
==Solution structure of the CR4/5 domain of medaka telomerase RNA==
 +
<StructureSection load='2mhi' size='340' side='right'caption='[[2mhi]]' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2mhi]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MHI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MHI FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mhi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mhi OCA], [https://pdbe.org/2mhi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mhi RCSB], [https://www.ebi.ac.uk/pdbsum/2mhi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mhi ProSAT]</span></td></tr>
 +
</table>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Telomerase is a unique reverse transcriptase that maintains the 3' ends of eukaryotic chromosomes by adding tandem telomeric repeats. The RNA subunit (TR) of vertebrate telomerase provides a template for reverse transcription, contained within the conserved template/pseudoknot domain, and a conserved regions 4 and 5 (CR4/5) domain, all essential for catalytic activity. We report the nuclear magnetic resonance (NMR) solution structure of the full-length CR4/5 domain from the teleost fish medaka (Oryzias latipes). Three helices emanate from a structured internal loop, forming a Y-shaped structure, where helix P6 stacks on P5 and helix P6.1 points away from P6. The relative orientations of the three helices are Mg2+ dependent and dynamic. Although the three-way junction is structured and has unexpected base pairs, telomerase activity assays with nucleotide substitutions and deletions in CR4/5 indicate that none of these are essential for activity. The results suggest that the junction is likely to change conformation in complex with telomerase reverse transcriptase and that it provides a flexible scaffold that allows P6 and P6.1 to correctly fold and interact with telomerase reverse transcriptase.
-
Authors: Kim, N., Zhang, Q., Feigon, J.
+
Structure and sequence elements of the CR4/5 domain of medaka telomerase RNA important for telomerase function.,Kim NK, Zhang Q, Feigon J Nucleic Acids Res. 2013 Dec 11. PMID:24335084<ref>PMID:24335084</ref>
-
Description: Hold for publication
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 2mhi" style="background-color:#fffaf0;"></div>
 +
 
 +
==See Also==
 +
*[[Telomerase 3D structures|Telomerase 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Feigon J]]
 +
[[Category: Kim N]]
 +
[[Category: Zhang Q]]

Current revision

Solution structure of the CR4/5 domain of medaka telomerase RNA

PDB ID 2mhi

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools