5LYN

Structure of the Tpr Domain of Sgt2 in complex with yeast Ssa1 peptide fragment

Summary for 5LYN

• Entry DOI: 10.2210/pdb5lyn/pdb
• Descriptor: Small glutamine-rich tetratricopeptide repeat-containing protein 2, PRO-THR-VAL-GLU-GLU-VAL-ASP, ZINC ION, ... (4 entities in total)
• Functional Keywords: chaperone
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Cytoplasm : Q12118
• Total number of polymer chains: 4
• Total formula weight: 31807.60

Authors

Krysztofinska, E.M.,Evans, N.J.,Thapaliya, A.,Murray, J.W.,Morgan, R.M.L.,Martinez-Lumbreras, S.,Isaacson, R.L. (deposition date: 2016-09-28, release date: 2017-10-25, Last modification date: 2024-01-17)

Primary citation

Krysztofinska, E.M.,Evans, N.J.,Thapaliya, A.,Murray, J.W.,Morgan, R.M.L.,Martinez-Lumbreras, S.,Isaacson, R.L.
Structure and Interactions of the TPR Domain of Sgt2 with Yeast Chaperones and Ybr137wp.
Front Mol Biosci, 4:68-68, 2017

PubMed Abstract: Small glutamine-rich tetratricopeptide repeat-containing protein 2 (Sgt2) is a multi-module co-chaperone involved in several protein quality control pathways. The TPR domain of Sgt2 and several other proteins, including SGTA, Hop, and CHIP, is a highly conserved motif known to form transient complexes with molecular chaperones such as Hsp70 and Hsp90. In this work, we present the first high resolution crystal structures of Sgt2_TPR alone and in complex with a C-terminal peptide PTVEEVD from heat shock protein, Ssa1. Using nuclear magnetic resonance spectroscopy and isothermal titration calorimetry, we demonstrate that Sgt2_TPR interacts with peptides corresponding to the C-termini of Ssa1, Hsc82, and Ybr137wp with similar binding modes and affinities.

PubMed: 29075633
DOI: 10.3389/fmolb.2017.00068

Experimental method

X-RAY DIFFRACTION (2 Å)