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Structure and Interactions of the TPR Domain of Sgt2 with Yeast Chaperones and Ybr137wp

DOI: 10.3389/fmolb.2017.00068 DOI Help

Authors: Ewelina M. Krysztofinska (King's College London) , Nicola J. Evans (King's College London) , Arjun Thapaliya (King's College London) , James Murray (Imperial College London) , Rhodri M. L. Morgan (Imperial College London) , Santiago Martinez-lumbreras (King's College London) , Rivka L. Isaacson (King's College London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Frontiers In Molecular Biosciences , VOL 4

State: Published (Approved)
Published: October 2017
Diamond Proposal Number(s): 12579 , 13597

Open Access Open Access

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.

Journal Keywords: Sgt2; TPR; carboxylate clamp; NMR; CSP; x-ray crystallography; ITC

Subject Areas: Biology and Bio-materials


Instruments: I03-Macromolecular Crystallography , I04-Macromolecular Crystallography

Documents:
fmolb-04-00068.pdf

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