6AZ0

Mitochondrial ATPase Protease YME1

6AZ0 の概要

• エントリーDOI: 10.2210/pdb6az0/pdb
• EMDBエントリー: 7023
• 分子名称: Mitochondrial inner membrane i-AAA protease supercomplex subunit YME1, poly(UNK), ADENOSINE-5'-TRIPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: mitochondrial, atpase, protease, hydrolase
• 由来する生物種: Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 291969.21

構造登録者

Puchades, C.,Rampello, A.J.,Shin, M.,Giuliano, C.,Wiseman, R.L.,Glynn, S.E.,Lander, G.C. (登録日: 2017-09-09, 公開日: 2017-11-15, 最終更新日: 2024-03-13)

主引用文献

Puchades, C.,Rampello, A.J.,Shin, M.,Giuliano, C.J.,Wiseman, R.L.,Glynn, S.E.,Lander, G.C.
Structure of the mitochondrial inner membrane AAA+ protease YME1 gives insight into substrate processing.
Science, 358:-, 2017

PubMed Abstract: We present an atomic model of a substrate-bound inner mitochondrial membrane AAA+ quality control protease in yeast, YME1. Our ~3.4-angstrom cryo-electron microscopy structure reveals how the adenosine triphosphatases (ATPases) form a closed spiral staircase encircling an unfolded substrate, directing it toward the flat, symmetric protease ring. Three coexisting nucleotide states allosterically induce distinct positioning of tyrosines in the central channel, resulting in substrate engagement and translocation to the negatively charged proteolytic chamber. This tight coordination by a network of conserved residues defines a sequential, around-the-ring adenosine triphosphate hydrolysis cycle that results in stepwise substrate translocation. A hingelike linker accommodates the large-scale nucleotide-driven motions of the ATPase spiral relative to the planar proteolytic base. The translocation mechanism is likely conserved for other AAA+ ATPases.

PubMed: 29097521
DOI: 10.1126/science.aao0464

実験手法

ELECTRON MICROSCOPY (3.4 Å)