4HCE

Crystal structure of the telomeric Saccharomyces cerevisiae Cdc13 OB2 domain

Summary for 4HCE

• Entry DOI: 10.2210/pdb4hce/pdb
• Descriptor: Cell division control protein 13 (2 entities in total)
• Functional Keywords: ob fold, oligonucleotide/oligosaccharide binding fold, cell cycle
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Cellular location: Chromosome, telomere: P32797
• Total number of polymer chains: 2
• Total formula weight: 33670.64

Authors

Mason, M.,Wannat, J.J.,Harper, S.,Schultz, D.C.,Speicher, D.W.,Johnson, F.B.,Skordalakes, E. (deposition date: 2012-09-29, release date: 2012-11-28, Last modification date: 2024-11-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.3 Å)