3NWT

Crystal structure of the N-terminal domain of the yeast telomere-binding and telomerase regulatory protein Cdc13

Summary for 3NWT

• Entry DOI: 10.2210/pdb3nwt/pdb
• Related: 3NWS
• Descriptor: Cell division control protein 13 (2 entities in total)
• Functional Keywords: oligonucleotide/oligosaccharide binding fold - ob fold, single stranded telomeric dna binding, cell cycle
• Biological source: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast)
• Total number of polymer chains: 1
• Total formula weight: 25158.83

Authors

Mitchell, M.T.,Smith, J.S.,Mason, M.,Harper, S.,Speicher, D.W.,Johnson, F.B.,Skordalakes, E. (deposition date: 2010-07-10, release date: 2010-09-22, Last modification date: 2024-02-21)

Primary citation

Mitchell, M.T.,Smith, J.S.,Mason, M.,Harper, S.,Speicher, D.W.,Johnson, F.B.,Skordalakes, E.
Cdc13 N-terminal dimerization, DNA binding, and telomere length regulation.
Mol.Cell.Biol., 30:5325-5334, 2010

PubMed Abstract: The essential yeast protein Cdc13 facilitates chromosome end replication by recruiting telomerase to telomeres, and together with its interacting partners Stn1 and Ten1, it protects chromosome ends from nucleolytic attack, thus contributing to genome integrity. Although Cdc13 has been studied extensively, the precise role of its N-terminal domain (Cdc13N) in telomere length regulation remains unclear. Here we present a structural, biochemical, and functional characterization of Cdc13N. The structure reveals that this domain comprises an oligonucleotide/oligosaccharide binding (OB) fold and is involved in Cdc13 dimerization. Biochemical data show that Cdc13N weakly binds long, single-stranded, telomeric DNA in a fashion that is directly dependent on domain oligomerization. When introduced into full-length Cdc13 in vivo, point mutations that prevented Cdc13N dimerization or DNA binding caused telomere shortening or lengthening, respectively. The multiple DNA binding domains and dimeric nature of Cdc13 offer unique insights into how it coordinates the recruitment and regulation of telomerase access to the telomeres.

PubMed: 20837709
DOI: 10.1128/MCB.00515-10

Experimental method

X-RAY DIFFRACTION (2.7 Å)