4FW9

Crystal structure of the Lon-like protease MtaLonC

4FW9 の概要

• エントリーDOI: 10.2210/pdb4fw9/pdb
• 関連するPDBエントリー: 4FWD 4FWG 4FWH
• 分子名称: TTC1975 peptidase, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: lon protease, hydrolase
• 由来する生物種: Meiothermus taiwanensis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 81017.67

構造登録者

Chang, C.I.,Ihara, K.,Kuo, C.I.,Huang, K.F.,Wakatsuki, S. (登録日: 2012-06-30, 公開日: 2013-06-26, 最終更新日: 2024-11-06)

主引用文献

Liao, J.H.,Ihara, K.,Kuo, C.I.,Huang, K.F.,Wakatsuki, S.,Wu, S.H.,Chang, C.I.
Structures of an ATP-independent Lon-like protease and its complexes with covalent inhibitors
Acta Crystallogr.,Sect.D, 69:1395-1402, 2013

PubMed Abstract: The Lon proteases are a unique family of chambered proteases with a built-in AAA+ (ATPases associated with diverse cellular activities) module. Here, crystal structures of a unique member of the Lon family with no intrinsic ATPase activity in the proteolytically active form are reported both alone and in complexes with three covalent inhibitors: two peptidomimetics and one derived from a natural product. This work reveals the unique architectural features of an ATP-independent Lon that selectively degrades unfolded protein substrates. Importantly, these results provide mechanistic insights into the recognition of inhibitors and polypeptide substrates within the conserved proteolytic chamber, which may aid the development of specific Lon-protease inhibitors.

PubMed: 23897463
DOI: 10.1107/S0907444913008214

実験手法

X-RAY DIFFRACTION (2 Å)