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Cited by 9Enzyme Structure and FunctionProtease and Inhibitor MechanismsPeptidase Inhibition and Analysis

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Structure of puromycin-sensitive aminopeptidase and polyglutamine binding

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Madabushi, Sowmya, Chow, K. Martin, Song, Eun Suk, Goswami, Anwesha, Hersh, Louis B., Rodgers, David W.·2023·PLOS ONE
DOI 10.1371/journal.pone.0287086PMC PMC10343166

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Abstract

Puromycin-sensitive aminopeptidase (E.C. 3.4.11.14, UniProt P55786), a zinc metallopeptidase belonging to the M1 family, degrades a number of bioactive peptides as well as peptides released from the proteasome, including polyglutamine. We report the crystal structure of PSA at 2.3 Ǻ. Overall, the enzyme adopts a V-shaped architecture with four domains characteristic of the M1 family aminopeptidases, but it is in a less compact conformation compared to most M1 enzymes of known structure. A microtubule binding sequence is present in a C-terminal HEAT repeat domain of the enzyme in a position where it might serve to mediate interaction with tubulin. In the catalytic metallopeptidase domain, an elongated active site groove lined with aromatic and hydrophobic residues and a large S1 subsite may play a role in broad substrate recognition. The structure with bound polyglutamine shows a possible interacting mode of this peptide, which is supported by mutation.

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Metadata

Authors
Madabushi, S., Chow, K. M., Song, E. S., Goswami, A., Hersh, L. B., & Rodgers, D. W.
Affiliations
University of Kentucky (US)
Corresponding author
Rodgers, David W.
ORCID
Venue
PLOS ONE
Publisher
Public Library of Science (PLoS)
Published
2023-07-13
Volume
18
Issue
7
Pages
e0287086
ISSN
1932-6203 (ISSN-L)
DOI
10.1371/journal.pone.0287086
PMC
PMC10343166
OpenAlex
W4384156328
Cited by
9
References
4
Citations by year
2026: 2 · 2025: 4 · 2024: 3
FWCI
0.66
Type
journal article
Language
en
Open access
Licence
Locations
  • PLoS ONE (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • National Institute of General Medical Sciences (GM130954)
  • National Institute of Neurological Disorders and Stroke (NS38041)
  • National Institute on Drug Abuse (DA02243)
  • National Science Foundation (IIA-1355438)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Peptidase Inhibition and Analysis
Keywords
puromycin-sensitive aminopeptidase, zinc metallopeptidase, crystal structure, microtubule binding, substrate recognition, S1 subsite, active site, peptide degradation
MeSH terms
Aminopeptidases, Binding Sites, Peptides, Substrate Specificity, Metalloproteases

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