5dfm: Difference between revisions
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==Structure of Tetrahymena telomerase p19 fused to MBP== | ==Structure of Tetrahymena telomerase p19 fused to MBP== | ||
<StructureSection load='5dfm' size='340' side='right' caption='[[5dfm]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='5dfm' size='340' side='right' caption='[[5dfm]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAL:MALTOSE'>MAL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAL:MALTOSE'>MAL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dfn|5dfn]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dfn|5dfn]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5dfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dfm OCA], [http://pdbe.org/5dfm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dfm RCSB], [http://www.ebi.ac.uk/pdbsum/5dfm PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5dfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dfm OCA], [http://pdbe.org/5dfm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dfm RCSB], [http://www.ebi.ac.uk/pdbsum/5dfm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dfm ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5dfm" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5dfm" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Telomerase-associated protein|Telomerase-associated protein]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 19:58, 18 August 2017
Structure of Tetrahymena telomerase p19 fused to MBPStructure of Tetrahymena telomerase p19 fused to MBP
Structural highlights
Function[MALE_ECO57] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides (By similarity). Publication Abstract from PubMedTelomerase helps maintain telomeres by processive synthesis of telomere repeat DNA at their 3'-ends, using an integral telomerase RNA (TER) and telomerase reverse transcriptase (TERT). We report the cryo-electron microscopy structure of Tetrahymena telomerase at ~9 angstrom resolution. In addition to seven known holoenzyme proteins, we identify two additional proteins that form a complex (TEB) with single-stranded telomere DNA-binding protein Teb1, paralogous to heterotrimeric replication protein A (RPA). The p75-p45-p19 subcomplex is identified as another RPA-related complex, CST (CTC1-STN1-TEN1). This study reveals the paths of TER in the TERT-TER-p65 catalytic core and single-stranded DNA exit; extensive subunit interactions of the TERT essential N-terminal domain, p50, and TEB; and other subunit identities and structures, including p19 and p45C crystal structures. Our findings provide structural and mechanistic insights into telomerase holoenzyme function. Structure of Tetrahymena telomerase reveals previously unknown subunits, functions, and interactions.,Jiang J, Chan H, Cash DD, Miracco EJ, Ogorzalek Loo RR, Upton HE, Cascio D, O'Brien Johnson R, Collins K, Loo JA, Zhou ZH, Feigon J Science. 2015 Oct 30;350(6260):aab4070. doi: 10.1126/science.aab4070. Epub 2015, Oct 15. PMID:26472759[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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