4HCE

Crystal structure of the telomeric Saccharomyces cerevisiae Cdc13 OB2 domain

4HCE の概要

• エントリーDOI: 10.2210/pdb4hce/pdb
• 分子名称: Cell division control protein 13 (2 entities in total)
• 機能のキーワード: ob fold, oligonucleotide/oligosaccharide binding fold, cell cycle
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• 細胞内の位置: Chromosome, telomere: P32797
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 33670.64

構造登録者

Mason, M.,Wannat, J.J.,Harper, S.,Schultz, D.C.,Speicher, D.W.,Johnson, F.B.,Skordalakes, E. (登録日: 2012-09-29, 公開日: 2012-11-28, 最終更新日: 2024-11-27)

主引用文献

Mason, M.,Wanat, J.J.,Harper, S.,Schultz, D.C.,Speicher, D.W.,Johnson, F.B.,Skordalakes, E.
Cdc13 OB2 Dimerization Required for Productive Stn1 Binding and Efficient Telomere Maintenance.
Structure, 21:109-120, 2013

PubMed Abstract: Cdc13 is an essential yeast protein required for telomere length regulation and genome stability. It does so via its telomere-capping properties and by regulating telomerase access to the telomeres. The crystal structure of the Saccharomyces cerevisiae Cdc13 domain located between the recruitment and DNA binding domains reveals an oligonucleotide-oligosaccharide binding fold (OB2) with unusually long loops extending from the core of the protein. These loops are involved in extensive interactions between two Cdc13 OB2 folds leading to stable homodimerization. Interestingly, the functionally impaired cdc13-1 mutation inhibits OB2 dimerization. Biochemical assays indicate OB2 is not involved in telomeric DNA or Stn1 binding. However, disruption of the OB2 dimer in full-length Cdc13 affects Cdc13-Stn1 association, leading to telomere length deregulation, increased temperature sensitivity, and Stn1 binding defects. We therefore propose that dimerization of the OB2 domain of Cdc13 is required for proper Cdc13, Stn1, Ten1 (CST) assembly and productive telomere capping.

PubMed: 23177925
DOI: 10.1016/j.str.2012.10.012

実験手法

X-RAY DIFFRACTION (2.3 Å)