Cryo-EM structure of acylpeptide hydrolase reveals substrate selection by multimerization and a multi-state serine-protease triad-Reference-Cited by-同舟云学术

Cryo-EM structure of acylpeptide hydrolase reveals substrate selection by multimerization and a multi-state serine-protease triad

Published:2022 Issue:24 Volume:13 Page:7132-7142
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Kiss-Szemán Anna J.¹^ORCID,Stráner Pál²^ORCID,Jákli Imre¹²^ORCID,Hosogi Naoki³^ORCID,Harmat Veronika¹²^ORCID,Menyhárd Dóra K.¹²^ORCID,Perczel András¹²^ORCID

Affiliation:

1. Laboratory of Structural Chemistry and Biology, Institute of Chemistry, Eötvös Loránd University, Budapest – 1117, Hungary

2. MTA-ELTE Protein Modelling Research Group, Eötvös Loránd Research Network, Budapest – 1117, Hungary

3. EM Application Department, EM Business Unit, JEOL Ltd, Tokyo 196-8556, Japan

Abstract

The structure of tetrameric mammalian acylaminoacyl peptidase – a key upstream regulator of the proteasome – was determined by cryo-EM (and elucidated by MD), showing a “shutters-and-channels” substrate selection apparatus created by oligomerization.

Funder

European Regional Development Fund

Magyar Tudományos Akadémia

Nemzeti Kutatási Fejlesztési és Innovációs Hivatal

Innovációs és Technológiai Minisztérium

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2022/SC/D2SC02276A

Reference60 articles.