2L42

The solution structure of Rap1 BRCT domain from Saccharomyces cerevisiae

Summary for 2L42

• Entry DOI: 10.2210/pdb2l42/pdb
• Descriptor: DNA-binding protein RAP1 (1 entity in total)
• Functional Keywords: rap1, brct domain, dna binding protein, protein binding
• Biological source: Saccharomyces cerevisiae (yeast)
• Cellular location: Nucleus: P11938
• Total number of polymer chains: 1
• Total formula weight: 12185.60

Authors

Zhang, W.,Zhang, J.,Tu, X. (deposition date: 2010-09-29, release date: 2011-01-26, Last modification date: 2024-05-01)

Primary citation

Zhang, W.,Zhang, J.,Zhang, X.,Xu, C.,Tu, X.
Solution structure of Rap1 BRCT domain from Saccharomyces cerevisiae reveals a novel fold
Biochem.Biophys.Res.Commun., 404:1055-1059, 2011

PubMed Abstract: Rap1 (repressor-activator protein 1) from Saccharomyces cerevisiae, containing a BRCT domain at its N-terminus, is a multifunctional protein that controls telomere function, silencing, and the activation of glycolytic and ribosomal protein genes. In this work, we determined the solution structure of Rap1 BRCT domain, which contains three β-strands and three α-helices. Structural comparison indicated that Rap1 BRCT domain adopts a global fold similar to other BRCT domains, implying some common structural aspects of BRCT domain family. On the other hand, Rap1 BRCT domain displays structural characteristics significantly different from other BRCT domains in that Rap1 BRCT domain adopts a rather flexible conformation with less secondary structure elements, revealing a novel fold of the BRCT domain family.

PubMed: 21187076
DOI: 10.1016/j.bbrc.2010.12.109

Experimental method

SOLUTION NMR