5lyp
From Proteopedia
Crystal structure of the Tpr Domain of Sgt2.
Structural highlights
FunctionSGT2_YEAST Co-chaperone that binds to the molecular chaperone Hsp70 (SSA1 and SSA2). Regulates Hsp70 ATPase activity (By similarity). Required for recovery from heat shock.[1] Publication Abstract from PubMedSmall 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. Structure and Interactions of the TPR Domain of Sgt2 with Yeast Chaperones and Ybr137wp.,Krysztofinska EM, Evans NJ, Thapaliya A, Murray JW, Morgan RML, Martinez-Lumbreras S, Isaacson RL Front Mol Biosci. 2017 Oct 11;4:68. doi: 10.3389/fmolb.2017.00068. eCollection, 2017. PMID:29075633[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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