Structural basis for distinct operational modes and protease activation in AAA+ protease Lon-Reference-Cited by-同舟云学术

Structural basis for distinct operational modes and protease activation in AAA+ protease Lon

Published:2020-05-22 Issue:21 Volume:6 Page:
ISSN:2375-2548
Container-title:Science Advances
language:en
Short-container-title:Sci. Adv.

Author:

Shin Mia¹²^ORCID,Puchades Cristina¹²^ORCID,Asmita Ananya³^ORCID,Puri Neha³,Adjei Eric³^ORCID,Wiseman R. Luke²^ORCID,Karzai A. Wali³,Lander Gabriel C.¹^ORCID

Affiliation:

1. Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.

2. Department of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA.

3. Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY 11794-5215, USA.

Abstract

Substrate-free and -bound states of Lon reveal distinct operational modes used by the enzyme to process protein substrates.

Funder

National Institutes of Health

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference88 articles.

1. EVOLUTIONARY RELATIONSHIPS AND STRUCTURAL MECHANISMS OF AAA+ PROTEINS

2. AAA+ proteins: have engine, will work

3. Evolutionary history and higher order classification of AAA+ ATPases

4. AAA+ Proteases: ATP-Fueled Machines of Protein Destruction

5. Stairway to translocation: AAA+ motor structures reveal the mechanisms of ATP‐dependent substrate translocation

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