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=EST3=
=2m9v=
==Structure of Saccharomyces cerevisiae Est3 protein==
==Structure of Saccharomyces cerevisiae Est3 protein==
<StructureSection load='2m9v' size='340' side='right' caption='[[2m9v]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='2m9v' size='340' side='right' caption='[[2m9v]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
== Structural highlights ==
This is <scene name='75/752271/2f6a/2'>2f6a
This is <scene name='75/752271/2f6a/2'>2f6a
Deletion of 12 N-terminal residues, found to constitute this flexible region. The mutagenesis of the putative nonconserved surface cysteine residues (Cys64, Cys76, Cys109, and Cys142) which are identified as Cys 142Ser
<ref>DOI:10.1073/pnas.1316453111</ref>


</StructureSection>
</StructureSection>
== References ==
== References ==
<references/>
<references/>

Revision as of 22:57, 16 November 2020

2m9v2m9v

Structure of Saccharomyces cerevisiae Est3 proteinStructure of Saccharomyces cerevisiae Est3 protein

This is a default text for your page Sandbox GGC9. Click above on edit this page to modify. Be careful with the < and > signs.

You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.

Introduction

Telomerase is essential for continuous cellular proliferation. Substantial insights have come from studies of budding yeast telomerase. In cells that lack telomerase, gradual erosion due to incomplete replication of duplex telomeric DNA leads to an eventual Block to cellular proliferation.[3]

Function

A single pathway for telomere replication in the yeast Saccharomyces cerevisiae [4]

They have been studies about individual functions of the components of the S. cerevisiae telomerase.[5] Component of telomerase complex involved in telomere replication. Stimulates RNA/DNA heteroduplex unwinding which favors the telomere replication by the telomerase.[6] Est3 protein surface has an important opening up in the structurally similar human TPP1 protein. [7]

Disease

Saccharomyces cerevisiae is a species of yeast that is known in baking and brewing. Also, it is used as a probiotic in humans but it very uncommon infection in humans.[8]

Relevance

Studies have found Est3 adopts OB-fold with certain distinctive features. In most cases, the most notable discrepancy between Est and other OB-fold protein is OB-fold ligand-binding.[9]

Structural highlights

This is <scene name='75/752271/2f6a/2'>2f6a

Deletion of 12 N-terminal residues, found to constitute this flexible region. The mutagenesis of the putative nonconserved surface cysteine residues (Cys64, Cys76, Cys109, and Cys142) which are identified as Cys 142Ser [10]


Drag the structure with the mouse to rotate

ReferencesReferences

  1. ↑ Rao T, Lubin JW, Armstrong GS, Tucey TM, Lundblad V, Wuttke DS. Structure of Est3 reveals a bimodal surface with differential roles in telomere replication. 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 doi:http://dx.doi.org/10.1073/pnas.1316453111
  2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
  3. ↑ Rao T, Lubin JW, Armstrong GS, Tucey TM, Lundblad V, Wuttke DS. Structure of Est3 reveals a bimodal surface with differential roles in telomere replication. 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 doi:http://dx.doi.org/10.1073/pnas.1316453111
  4. ↑ DOI:10.1016/s0960-9822(00)00562-5
  5. ↑ 10.1093/nar/gkp1173
  6. ↑ Rao T, Lubin JW, Armstrong GS, Tucey TM, Lundblad V, Wuttke DS. Structure of Est3 reveals a bimodal surface with differential roles in telomere replication. 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 doi:http://dx.doi.org/10.1073/pnas.1316453111
  7. ↑ Rao T, Lubin JW, Armstrong GS, Tucey TM, Lundblad V, Wuttke DS. Structure of Est3 reveals a bimodal surface with differential roles in telomere replication. 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 doi:http://dx.doi.org/10.1073/pnas.1316453111
  8. ↑ https://doi.org/10.1086/429916
  9. ↑ Rao T, Lubin JW, Armstrong GS, Tucey TM, Lundblad V, Wuttke DS. Structure of Est3 reveals a bimodal surface with differential roles in telomere replication. 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 doi:http://dx.doi.org/10.1073/pnas.1316453111
  10. ↑ Rao T, Lubin JW, Armstrong GS, Tucey TM, Lundblad V, Wuttke DS. Structure of Est3 reveals a bimodal surface with differential roles in telomere replication. 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 doi:http://dx.doi.org/10.1073/pnas.1316453111

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