Structure of puromycin-sensitive aminopeptidase and polyglutamine binding.

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 en...

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Main Authors: Sowmya Madabushi, K Martin Chow, Eun Suk Song, Anwesha Goswami, Louis B Hersh, David W Rodgers
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2023-01-01
Series:PLoS ONE
Online Access:https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0287086&type=printable
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author Sowmya Madabushi
K Martin Chow
Eun Suk Song
Anwesha Goswami
Louis B Hersh
David W Rodgers
author_facet Sowmya Madabushi
K Martin Chow
Eun Suk Song
Anwesha Goswami
Louis B Hersh
David W Rodgers
author_sort Sowmya Madabushi
collection DOAJ
description 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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spelling doaj-art-3b2f3daab1ff45f786b376cc55adf2b02025-08-20T02:12:30ZengPublic Library of Science (PLoS)PLoS ONE1932-62032023-01-01187e028708610.1371/journal.pone.0287086Structure of puromycin-sensitive aminopeptidase and polyglutamine binding.Sowmya MadabushiK Martin ChowEun Suk SongAnwesha GoswamiLouis B HershDavid W RodgersPuromycin-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.https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0287086&type=printable
spellingShingle Sowmya Madabushi
K Martin Chow
Eun Suk Song
Anwesha Goswami
Louis B Hersh
David W Rodgers
Structure of puromycin-sensitive aminopeptidase and polyglutamine binding.
PLoS ONE
title Structure of puromycin-sensitive aminopeptidase and polyglutamine binding.
title_full Structure of puromycin-sensitive aminopeptidase and polyglutamine binding.
title_fullStr Structure of puromycin-sensitive aminopeptidase and polyglutamine binding.
title_full_unstemmed Structure of puromycin-sensitive aminopeptidase and polyglutamine binding.
title_short Structure of puromycin-sensitive aminopeptidase and polyglutamine binding.
title_sort structure of puromycin sensitive aminopeptidase and polyglutamine binding
url https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0287086&type=printable
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