Structural conservation of the PIN domain active site across all domains of life

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Structural conservation of the PIN domain active site across all domains of life. / Senissar, M; Manav, M C; Brodersen, D E.

In: Protein Science, Vol. 26, No. 8, 2017, p. 1474-1492.

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Senissar, M ; Manav, M C ; Brodersen, D E. / Structural conservation of the PIN domain active site across all domains of life. In: Protein Science. 2017 ; Vol. 26, No. 8. pp. 1474-1492.

Bibtex

@article{6fb385cdb6cd4e4d94801e19a25a03f6,
title = "Structural conservation of the PIN domain active site across all domains of life",
abstract = "The PIN domain (Pil N-terminus) is a compact RNA-binding protein domain present in all domains of life. This 120-residue domain consists of a central and parallel β sheet surrounded by α helices, which together organise 4-5 acidic residues in an active site that binds one or more divalent metal ions and in many cases has endoribonuclease activity. In bacteria and archaea, the PIN domain is primarily associated with toxin-antitoxin loci, consisting of a toxin (the PIN domain nuclease) and an antitoxin that inhibits the function of the toxin under normal growth conditions. During nutritional or antibiotic stress, the antitoxin is proteolytically degraded causing activation of the PIN domain toxin leading to a dramatic reprogramming of cellular metabolism to cope with the new conditions. In eukaryotes, PIN domains are commonly found as parts of larger proteins and are involved in a range of processes involving RNA cleavage, including ribosomal RNA biogenesis and nonsense-mediated mRNA decay. In this review, we provide a comprehensive overview of the structural characteristics of the PIN domain and compare PIN domains from all domains of life in terms of structure, active site architecture, and activity. This article is protected by copyright. All rights reserved.",
keywords = "Journal Article, Review",
author = "M Senissar and Manav, {M C} and Brodersen, {D E}",
note = "{\circledC} 2017 The Protein Society.",
year = "2017",
doi = "10.1002/pro.3193",
language = "English",
volume = "26",
pages = "1474--1492",
journal = "Protein Science",
issn = "0961-8368",
publisher = "Wiley-Blackwell Publishing, Inc.",
number = "8",

}

RIS

TY - JOUR

T1 - Structural conservation of the PIN domain active site across all domains of life

AU - Senissar, M

AU - Manav, M C

AU - Brodersen, D E

N1 - © 2017 The Protein Society.

PY - 2017

Y1 - 2017

N2 - The PIN domain (Pil N-terminus) is a compact RNA-binding protein domain present in all domains of life. This 120-residue domain consists of a central and parallel β sheet surrounded by α helices, which together organise 4-5 acidic residues in an active site that binds one or more divalent metal ions and in many cases has endoribonuclease activity. In bacteria and archaea, the PIN domain is primarily associated with toxin-antitoxin loci, consisting of a toxin (the PIN domain nuclease) and an antitoxin that inhibits the function of the toxin under normal growth conditions. During nutritional or antibiotic stress, the antitoxin is proteolytically degraded causing activation of the PIN domain toxin leading to a dramatic reprogramming of cellular metabolism to cope with the new conditions. In eukaryotes, PIN domains are commonly found as parts of larger proteins and are involved in a range of processes involving RNA cleavage, including ribosomal RNA biogenesis and nonsense-mediated mRNA decay. In this review, we provide a comprehensive overview of the structural characteristics of the PIN domain and compare PIN domains from all domains of life in terms of structure, active site architecture, and activity. This article is protected by copyright. All rights reserved.

AB - The PIN domain (Pil N-terminus) is a compact RNA-binding protein domain present in all domains of life. This 120-residue domain consists of a central and parallel β sheet surrounded by α helices, which together organise 4-5 acidic residues in an active site that binds one or more divalent metal ions and in many cases has endoribonuclease activity. In bacteria and archaea, the PIN domain is primarily associated with toxin-antitoxin loci, consisting of a toxin (the PIN domain nuclease) and an antitoxin that inhibits the function of the toxin under normal growth conditions. During nutritional or antibiotic stress, the antitoxin is proteolytically degraded causing activation of the PIN domain toxin leading to a dramatic reprogramming of cellular metabolism to cope with the new conditions. In eukaryotes, PIN domains are commonly found as parts of larger proteins and are involved in a range of processes involving RNA cleavage, including ribosomal RNA biogenesis and nonsense-mediated mRNA decay. In this review, we provide a comprehensive overview of the structural characteristics of the PIN domain and compare PIN domains from all domains of life in terms of structure, active site architecture, and activity. This article is protected by copyright. All rights reserved.

KW - Journal Article

KW - Review

U2 - 10.1002/pro.3193

DO - 10.1002/pro.3193

M3 - Journal article

C2 - 28508407

VL - 26

SP - 1474

EP - 1492

JO - Protein Science

JF - Protein Science

SN - 0961-8368

IS - 8

ER -