5LYP
Crystal structure of the Tpr Domain of Sgt2.
Summary for 5LYP
| Entry DOI | 10.2210/pdb5lyp/pdb |
| Descriptor | Small glutamine-rich tetratricopeptide repeat-containing protein 2, BORATE ION (3 entities in total) |
| Functional Keywords | chaperone |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Cellular location | Cytoplasm : Q12118 |
| Total number of polymer chains | 1 |
| Total formula weight | 15718.31 |
| Authors | Krysztofinska, E.M.,Morgan, R.M.L.,Thapaliya, A.,Evans, N.J.,Murray, J.W.,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 Cited by 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: 29075633DOI: 10.3389/fmolb.2017.00068 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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