5HPH

Structure of TRAP1 fragment

5HPH の概要

• エントリーDOI: 10.2210/pdb5hph/pdb
• 分子名称: Heat shock protein 75 kDa, mitochondrial, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, PHOSPHATE ION, ... (7 entities in total)
• 機能のキーワード: trap1, hsp90, chaperone
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 115811.56

構造登録者

Sung, N.,Chang, C.,Lee, S.,Tsai, F.T.F. (登録日: 2016-01-20, 公開日: 2016-08-10, 最終更新日: 2024-03-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.429 Å)