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5NVR

Crystal structure of the Rif1 N-terminal domain (RIF1-NTD) from Saccharomyces cerevisiae

Summary for 5NVR
Entry DOI10.2210/pdb5nvr/pdb
DescriptorTelomere length regulator protein RIF1 (1 entity in total)
Functional Keywordstelomere maintenance, dna double-strand break repair, irregular helical repeat, all-alpha fold, structural protein
Biological sourceSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Total number of polymer chains1
Total formula weight129054.05
Authors
Bunker, R.D.,Shi, T.,Thoma, N.H. (deposition date: 2017-05-04, release date: 2017-06-14, Last modification date: 2019-04-03)
Primary citationMattarocci, S.,Reinert, J.K.,Bunker, R.D.,Fontana, G.A.,Shi, T.,Klein, D.,Cavadini, S.,Faty, M.,Shyian, M.,Hafner, L.,Shore, D.,Thoma, N.H.,Rass, U.
Rif1 maintains telomeres and mediates DNA repair by encasing DNA ends.
Nat. Struct. Mol. Biol., 24:588-595, 2017
Cited by
PubMed: 28604726
DOI: 10.1038/nsmb.3420
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.95 Å)
Structure validation

218853

数据于2024-04-24公开中

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