5HPH

Structure of TRAP1 fragment

Summary for 5HPH

• Entry DOI: 10.2210/pdb5hph/pdb
• Descriptor: Heat shock protein 75 kDa, mitochondrial, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, PHOSPHATE ION, ... (7 entities in total)
• Functional Keywords: trap1, hsp90, chaperone
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 115811.56

Authors

Sung, N.,Chang, C.,Lee, S.,Tsai, F.T.F. (deposition date: 2016-01-20, release date: 2016-08-10, Last modification date: 2024-03-06)

Primary citation

Sung, N.,Lee, J.,Kim, J.H.,Chang, C.,Tsai, F.T.,Lee, S.
2.4 angstrom resolution crystal structure of human TRAP1NM, the Hsp90 paralog in the mitochondrial matrix.
Acta Crystallogr D Struct Biol, 72:904-911, 2016

PubMed Abstract: TRAP1 is an organelle-specific Hsp90 paralog that is essential for neoplastic growth. As a member of the Hsp90 family, TRAP1 is presumed to be a general chaperone facilitating the late-stage folding of Hsp90 client proteins in the mitochondrial matrix. Interestingly, TRAP1 cannot replace cytosolic Hsp90 in protein folding, and none of the known Hsp90 co-chaperones are found in mitochondria. Thus, the three-dimensional structure of TRAP1 must feature regulatory elements that are essential to the ATPase activity and chaperone function of TRAP1. Here, the crystal structure of a human TRAP1NM dimer is presented, featuring an intact N-domain and M-domain structure, bound to adenosine 5'-β,γ-imidotriphosphate (ADPNP). The crystal structure together with epitope-mapping results shows that the TRAP1 M-domain loop 1 contacts the neighboring subunit and forms a previously unobserved third dimer interface that mediates the specific interaction with mitochondrial Hsp70.

PubMed: 27487821
DOI: 10.1107/S2059798316009906

Experimental method

X-RAY DIFFRACTION (2.429 Å)