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Solution structure of a yeast ubiquitin‐like protein Smt3: The role of structurally less defined sequences in protein–protein recognitions
Author(s) -
Sheng Wanyun,
Liao Xiubei
Publication year - 2002
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.0201602
Subject(s) - yeast , ubiquitin , protein stability , protein structure , biology , biochemistry , chemistry , protein structure prediction , microbiology and biotechnology , gene
Smt3 belongs to a growing family of ubiquitin‐related proteins involved in posttranslational protein modification. Independent studies demonstrate an essential function of Smt3 in the regulation of nucleocytoplasmic transport, and suggest a role in cell‐cycle regulation. Here we report the high‐resolution NMR structure of yeast Smt3 in the complex free form. Our comparison of the Smt3 NMR structure with the Smt3 crystal structure in complex with the C‐Terminal Ulp1 protease domain revealed large structural differences in the binding surface, which is also involved in the Smt3‐Ubc‐9 interaction detected by NMR. The structural differences in the region indicate the important functions of conserved residues in less structurally defined sequences.