6AZ0

Mitochondrial ATPase Protease YME1

Summary for 6AZ0

• Entry DOI: 10.2210/pdb6az0/pdb
• EMDB information: 7023
• Descriptor: Mitochondrial inner membrane i-AAA protease supercomplex subunit YME1, poly(UNK), ADENOSINE-5'-TRIPHOSPHATE, ... (6 entities in total)
• Functional Keywords: mitochondrial, atpase, protease, hydrolase
• Biological source: Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast); More
• Total number of polymer chains: 7
• Total formula weight: 291969.21

Authors

Puchades, C.,Rampello, A.J.,Shin, M.,Giuliano, C.,Wiseman, R.L.,Glynn, S.E.,Lander, G.C. (deposition date: 2017-09-09, release date: 2017-11-15, Last modification date: 2024-03-13)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (3.4 Å)