3KDS

apo-FtsH crystal structure

3KDS の概要

• エントリーDOI: 10.2210/pdb3kds/pdb
• 関連するPDBエントリー: 2CE7 2CEA
• 分子名称: Cell division protein FtsH, ZINC ION, N-{(2R)-2-[2-(hydroxyamino)-2-oxoethyl]-4-methylpentanoyl}-3-naphthalen-2-yl-L-alanyl-L-alaninamide (3 entities in total)
• 機能のキーワード: met-turn, beta roll, metal binding protein
• 由来する生物種: Thermotoga maritima
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein; Cytoplasmic side (By similarity): Q9WZ49
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 155807.65

構造登録者

Bieniossek, C.,Niederhauser, B.,Baumann, U. (登録日: 2009-10-23, 公開日: 2009-12-01, 最終更新日: 2023-11-01)

主引用文献

Bieniossek, C.,Niederhauser, B.,Baumann, U.M.
The crystal structure of apo-FtsH reveals domain movements necessary for substrate unfolding and translocation
Proc.Natl.Acad.Sci.USA, 106:21579-21584, 2009

PubMed Abstract: The hexameric membrane-spanning ATP-dependent metalloprotease FtsH is universally conserved in eubacteria, mitochondria, and chloroplasts, where it fulfills key functions in quality control and signaling. As a member of the self-compartmentalizing ATPases associated with various cellular activities (AAA+ proteases), FtsH converts the chemical energy stored in ATP via conformational rearrangements into a mechanical force that is used for substrate unfolding and translocation into the proteolytic chamber. The crystal structure of the ADP state of Thermotoga maritima FtsH showed a hexameric assembly consisting of a 6-fold symmetric protease disk and a 2-fold symmetric AAA ring. The 2.6 A resolution structure of the cytosolic region of apo-FtsH presented here reveals a new arrangement where the ATPase ring shows perfect 6-fold symmetry with the crucial pore residues lining an open circular entrance. Triggered by this conformational change, a substrate-binding edge beta strand appears within the proteolytic domain. Comparison of the apo- and ADP-bound structure visualizes an inward movement of the aromatic pore residues and generates a model of substrate translocation by AAA+ proteases. Furthermore, we demonstrate that mutation of a conserved glycine in the linker region inactivates FtsH.

PubMed: 19955424
DOI: 10.1073/pnas.0910708106

実験手法

X-RAY DIFFRACTION (2.601 Å)