1L2N

Smt3 Solution Structure

Summary for 1L2N

• Entry DOI: 10.2210/pdb1l2n/pdb
• Descriptor: Ubiquitin-like protein SMT3 (1 entity in total)
• Functional Keywords: smt3, ubiquitin-like protein, protein binding
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 1
• Total formula weight: 11614.04

Authors

Sheng, W.,Liao, X. (deposition date: 2002-02-22, release date: 2002-03-06, Last modification date: 2024-05-22)

Primary citation

Sheng, W.,Liao, X.
Solution structure of a yeast ubiquitin-like protein Smt3: the role of structurally less defined sequences in protein-protein recognitions.
Protein Sci., 11:1482-1491, 2002

PubMed Abstract: 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.

PubMed: 12021447
DOI: 10.1110/ps.0201602

Experimental method

SOLUTION NMR