Abstract:
:Hsp70 chaperone proteins play crucial roles in the cell. Extensive structural and functional studies have been performed for bacterial and mammalian Hsp70s. Ssa1 from Saccharomyces cerevisiae is a member of the Hsp70 family. In vivo and biochemical studies on Ssa1 have revealed that it regulates prion propagation and the cell cycle. However, no structural data has been obtained for Ssa1 up to now. Here we report the almost complete (96 %) (1)H, (13)C, (15)N backbone and side chain NMR assignment of the 18.8 kDa Ssa1 substrate binding domain. The construct includes residues 382-554, which corresponds to the entire substrate binding domain and two following α-helices in homologous structures. The secondary structure predicted from the assigned chemical shifts is consistent with that of homologous Hsp70 substrate binding domains.
journal_name
Biomol NMR Assignjournal_title
Biomolecular NMR assignmentsauthors
Hu W,Wu H,Zhang H,Gong W,Perrett Sdoi
10.1007/s12104-015-9603-5subject
Has Abstractpub_date
2015-10-01 00:00:00pages
329-32issue
2eissn
1874-2718issn
1874-270Xpii
10.1007/s12104-015-9603-5journal_volume
9pub_type
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