2m9v: Difference between revisions
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==Structure of Saccharomyces cerevisiae Est3 protein== | |||
===Structure of | <StructureSection load='2m9v' size='340' side='right' caption='[[2m9v]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2m9v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M9V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2M9V FirstGlance]. <br> | |||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EST3, YIL009C-A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=2m9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m9v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2m9v RCSB], [http://www.ebi.ac.uk/pdbsum/2m9v PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Telomerase is essential for continuous cellular proliferation. Substantial insights have come from studies of budding yeast telomerase, which consists of a catalytic core in association with two regulatory proteins, ever shorter telomeres 1 and 3 (Est1 and Est3). We report here a high-resolution structure of the Est3 telomerase subunit determined using a recently developed strategy that combines minimal NMR experimental data with Rosetta de novo structure prediction algorithms. Est3 adopts an overall protein fold which is structurally similar to that adopted by the shelterin component TPP1. However, the characteristics of the surface of the experimentally determined Est3 structure are substantially different from those predicted by prior homology-based models of Est3. Structure-guided mutagenesis of the complete surface of the Est3 protein reveals two adjacent patches on a noncanonical face of the protein that differentially mediate telomere function. Mapping these two patches on the Est3 structure defines a set of shared features between Est3 and HsTPP1, suggesting an analogous multifunctional surface on TPP1. | |||
Structure of Est3 reveals a bimodal surface with differential roles in telomere replication.,Rao T, Lubin JW, Armstrong GS, Tucey TM, Lundblad V, Wuttke DS Proc Natl Acad Sci U S A. 2014 Jan 7;111(1):214-8. doi: 10.1073/pnas.1316453111. , Epub 2013 Dec 16. PMID:24344315<ref>PMID:24344315</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
[[Category: Armstrong, G S | </StructureSection> | ||
[[Category: Rao, T | [[Category: Baker's yeast]] | ||
[[Category: Wuttke, D S | [[Category: Armstrong, G S]] | ||
[[Category: Rao, T]] | |||
[[Category: Wuttke, D S]] | |||
[[Category: Protein binding]] | [[Category: Protein binding]] | ||
Revision as of 21:17, 21 December 2014
Structure of Saccharomyces cerevisiae Est3 proteinStructure of Saccharomyces cerevisiae Est3 protein
Structural highlights
Publication Abstract from PubMedTelomerase is essential for continuous cellular proliferation. Substantial insights have come from studies of budding yeast telomerase, which consists of a catalytic core in association with two regulatory proteins, ever shorter telomeres 1 and 3 (Est1 and Est3). We report here a high-resolution structure of the Est3 telomerase subunit determined using a recently developed strategy that combines minimal NMR experimental data with Rosetta de novo structure prediction algorithms. Est3 adopts an overall protein fold which is structurally similar to that adopted by the shelterin component TPP1. However, the characteristics of the surface of the experimentally determined Est3 structure are substantially different from those predicted by prior homology-based models of Est3. Structure-guided mutagenesis of the complete surface of the Est3 protein reveals two adjacent patches on a noncanonical face of the protein that differentially mediate telomere function. Mapping these two patches on the Est3 structure defines a set of shared features between Est3 and HsTPP1, suggesting an analogous multifunctional surface on TPP1. Structure of Est3 reveals a bimodal surface with differential roles in telomere replication.,Rao T, Lubin JW, Armstrong GS, Tucey TM, Lundblad V, Wuttke DS Proc Natl Acad Sci U S A. 2014 Jan 7;111(1):214-8. doi: 10.1073/pnas.1316453111. , Epub 2013 Dec 16. PMID:24344315[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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