2BUG

Solution structure of the TPR domain from Protein phosphatase 5 in complex with Hsp90 derived peptide

Summary for 2BUG

• Entry DOI: 10.2210/pdb2bug/pdb
• Related: 1A17 1S95 1WAO
• NMR Information: BMRB: 6696
• Descriptor: SERINE/THREONINE PROTEIN PHOSPHATASE 5, HSP90 (2 entities in total)
• Functional Keywords: tetratricopeptide domain, protein phosphatase, hsp90 binding, hydrolase, iron, manganese, metal-binding
• Biological source: HOMO SAPIENS (HUMAN); More
• Total number of polymer chains: 2
• Total formula weight: 16859.09

Authors

Cliff, M.J.,Harris, R.,Barford, D.,Ladbury, J.E.,Williams, M.A. (deposition date: 2005-06-13, release date: 2006-03-16, Last modification date: 2020-01-15)

Primary citation

Cliff, M.J.,Harris, R.,Barford, D.,Ladbury, J.E.,Williams, M.A.
Conformational Diversity in the Tpr Domain-Mediated Interaction of Protein Phosphatase 5 with Hsp90.
Structure, 14:415-, 2006

PubMed Abstract: Protein phosphatase 5 (Ppp5) is one of several proteins that bind to the Hsp90 chaperone via a tetratricopeptide repeat (TPR) domain. We report the solution structure of a complex of the TPR domain of Ppp5 with the C-terminal pentapeptide of Hsp90. This structure has the "two-carboxylate clamp" mechanism of peptide binding first seen in the Hop-TPR domain complexes with Hsp90 and Hsp70 peptides. However, NMR data reveal that the Ppp5 clamp is highly dynamic, and that there are multiple modes of peptide binding and mobility throughout the complex. Although this interaction is of very high affinity, relatively few persistent contacts are found between the peptide and the Ppp5-TPR domain, thus explaining its promiscuity in binding both Hsp70 and Hsp90 in vivo. We consider the possible implications of this dynamic structure for the mechanism of relief of autoinhibition in Ppp5 and for the mechanisms of TPR-mediated recognition of Hsp90 by other proteins.

PubMed: 16531226
DOI: 10.1016/J.STR.2005.12.009

Experimental method

SOLUTION NMR