4o26: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(5 intermediate revisions by the same user not shown)
Line 1: Line 1:
==Crystal structure of the TRBD domain of TERT and the CR4/5 of TR==
==Crystal structure of the TRBD domain of TERT and the CR4/5 of TR==
<StructureSection load='4o26' size='340' side='right' caption='[[4o26]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='4o26' size='340' side='right'caption='[[4o26]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4o26]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O26 OCA]. <br>
<table><tr><td colspan='2'>[[4o26]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryzias_latipes Oryzias latipes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O26 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O26 FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.001&#8491;</td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4o26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o26 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o26 RCSB], [http://www.ebi.ac.uk/pdbsum/4o26 PDBsum]</span></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=4o26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o26 OCA], [https://pdbe.org/4o26 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o26 RCSB], [https://www.ebi.ac.uk/pdbsum/4o26 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o26 ProSAT]</span></td></tr>
<table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TERT_ORYLA TERT_ORYLA] Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres. It is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme.<ref>PMID:18039659</ref> <ref>PMID:22123986</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Telomerase is a large ribonucleoprotein complex minimally composed of a catalytic telomerase reverse transcriptase (TERT) and an RNA component (TR) that provides the template for telomeric DNA synthesis. However, it remains unclear how TERT and TR assemble into a functional telomerase. Here we report the crystal structure of the conserved regions 4 and 5 (CR4/5) of TR in complex with the TR-binding domain (TRBD) of TERT from the teleost fish Oryzias latipes. The structure shows that CR4/5 adopts an L-shaped three-way-junction conformation with its two arms clamping onto TRBD. Both the sequence and conformation of CR4/5 are required for the interaction. Our structural and mutational analyses suggest that the observed CR4/5-TRBD recognition is common to most eukaryotes, and CR4/5 in vertebrate TR might have a similar role in telomerase regulation as that of stem-loop IV in Tetrahymena TR.
 
Structural basis for protein-RNA recognition in telomerase.,Huang J, Brown AF, Wu J, Xue J, Bley CJ, Rand DP, Wu L, Zhang R, Chen JJ, Lei M Nat Struct Mol Biol. 2014 Jun;21(6):507-12. doi: 10.1038/nsmb.2819. Epub 2014 May, 4. PMID:24793650<ref>PMID:24793650</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4o26" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Telomerase 3D structures|Telomerase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Huang, J.]]
[[Category: Large Structures]]
[[Category: Lei, M.]]
[[Category: Oryzias latipes]]
[[Category: Wu, J.]]
[[Category: Huang J]]
[[Category: Protein-rna interaction]]
[[Category: Lei M]]
[[Category: Rna binding protein-rna complex]]
[[Category: Wu J]]
[[Category: Telomerase]]
[[Category: Telomerase rna]]

Latest revision as of 10:21, 30 October 2024

Crystal structure of the TRBD domain of TERT and the CR4/5 of TR

4o26, resolution 3.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA