2M9V

Structure of Saccharomyces cerevisiae Est3 protein

Summary for 2M9V

• Entry DOI: 10.2210/pdb2m9v/pdb
• NMR Information: BMRB: 19311
• Descriptor: Telomere replication protein EST3 (1 entity in total)
• Functional Keywords: protein binding
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Cellular location: Nucleus (Probable): Q03096
• Total number of polymer chains: 1
• Total formula weight: 19297.86

Authors

Rao, T.,Armstrong, G.S.,Wuttke, D.S. (deposition date: 2013-06-21, release date: 2013-12-18, Last modification date: 2024-05-15)

Primary citation

Rao, T.,Lubin, J.W.,Armstrong, G.S.,Tucey, T.M.,Lundblad, V.,Wuttke, D.S.
Structure of Est3 reveals a bimodal surface with differential roles in telomere replication.
Proc.Natl.Acad.Sci.USA, 111:214-218, 2014

PubMed Abstract: 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.

PubMed: 24344315
DOI: 10.1073/pnas.1316453111

Experimental method

SOLUTION NMR