Solution structure of a yeast ubiquitin-like prote...[Protein Sci. 2002]

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1: Protein Sci. 2002 Jun;11(6):1482-91. Links

Solution structure of a yeast ubiquitin-like protein Smt3: the role of structurally less defined sequences in protein-protein recognitions.

Sheng W, Liao X.

Department of Biochemistry and Molecular Biology, College of Medicine, University of Illinois, Chicago, Illinois 60612-4316, USA.

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.

PMID: 12021447 [PubMed - indexed for MEDLINE]

PMCID: PMC2373614

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[Mol Cell Biol. 2000]
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Cited by 1 PubMed Central article

Structure of a SUMO-binding-motif mimic bound to Smt3p-Ubc9p: conservation of a non-covalent ubiquitin-like protein-E2 complex as a platform for selective interactions within a SUMO pathway.
Duda DM, van Waardenburg RC, Borg LA, McGarity S, Nourse A, Waddell MB, Bjornsti MA, Schulman BA. J Mol Biol. 2007 Jun 8; 369(3):619-30. Epub 2007 Apr 10.

[J Mol Biol. 2007]

Structures reported by this article

Smt3 Solution Structure

PDB: 1L2N

Source: Saccharomyces cerevisiae

Method: Nmr, 20 Structures

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