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In molecular biology the '''PIN domain''' is a [[protein domain]] that is about 130 amino acids in length. The PIN domain was named after its identification in the N-nerminus of the PilT protein ('''Pi'''lT '''N''' terminus). PIN domains function as [[nuclease]] enzymes that cleave [[ssRNA|single stranded RNA]] in a sequence dependent manner.<ref name="pmid21036780">{{cite journal |author=Arcus VL, McKenzie JL, Robson J, Cook GM |title=The PIN-domain ribonucleases and the prokaryotic VapBC toxin-antitoxin array |journal=Protein Eng. Des. Sel. |volume=24 |issue=1-2 |pages=33–40 |year=2011 |month=January |pmid=21036780 |doi=10.1093/protein/gzq081 |url=}}</ref>
In molecular biology the '''PIN domain''' is a [[protein domain]] that is about 130 amino acids in length. The PIN domain was named after its identification in the N-nerminus of the PilT protein ('''Pi'''lT '''N''' terminus). PIN domains function as [[nuclease]] enzymes that cleave [[ssRNA|single stranded RNA]] in a sequence dependent manner.<ref name="pmid21036780">{{cite journal |author=Arcus VL, McKenzie JL, Robson J, Cook GM |title=The PIN-domain ribonucleases and the prokaryotic VapBC toxin-antitoxin array |journal=Protein Eng. Des. Sel. |volume=24 |issue=1-2 |pages=33–40 |year=2011 |month=January |pmid=21036780 |doi=10.1093/protein/gzq081 |url=}}</ref>


PIN domains contain three nearly invariant acidic residues. Crystal structures show these residues clustered together in the putative [[active site]]. In eukaryotes PIN domains are found in proteins involved in [[nonsense mediated decay|nonsense mediated mRNA decay]], in proteins such as [[SMG5]] and [[SMG6]], and in processing of 18S [[ribosomal RNA]]. The majority of PIN-domain proteins found in prokaryotes are the toxic components of toxin-antitoxin operon, and toxin-antitoxin gene cassettes, These loci provide a control mechanism that helps free-living prokaryotes cope with nutritional stress.<ref name="pmid15864262">{{cite journal |author=Gerdes K, Christensen SK, Løbner-Olesen A |title=Prokaryotic toxin-antitoxin stress response loci |journal=Nat. Rev. Microbiol. |volume=3 |issue=5 |pages=371–82 |year=2005 |month=May |pmid=15864262 |doi=10.1038/nrmicro1147 |url=}}</ref>
PIN domains contain three nearly invariant acidic residues. Crystal structures show these residues clustered together in the putative [[active site]]. In eukaryotes PIN domains are found in proteins involved in [[nonsense mediated decay|nonsense mediated mRNA decay]], in proteins such as [[SMG5]] and [[SMG6]], and in processing of 18S [[ribosomal RNA]]. The majority of PIN-domain proteins found in prokaryotes are the toxic components of [[toxin-antitoxin system|toxin-antitoxin operon]], and toxin-antitoxin gene cassettes, These loci provide a control mechanism that helps free-living prokaryotes cope with nutritional stress.<ref name="pmid15864262">{{cite journal |author=Gerdes K, Christensen SK, Løbner-Olesen A |title=Prokaryotic toxin-antitoxin stress response loci |journal=Nat. Rev. Microbiol. |volume=3 |issue=5 |pages=371–82 |year=2005 |month=May |pmid=15864262 |doi=10.1038/nrmicro1147 |url=}}</ref>


==References==
==References==

Revision as of 12:11, 9 May 2011

PIN domain
Crystal structure of PIN (PilT N-terminus) domain (AF0591) from Archaeoglobus fulgidus at 1.90 Angstrom resolution. 1o4w
Identifiers
SymbolPIN
PfamPF01850
InterProIPR002716
SMARTCBS
SCOP23dbo / SCOPe / SUPFAM
CDDcd09852
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB3dbo​, 1v8o​, 1o4w

In molecular biology the PIN domain is a protein domain that is about 130 amino acids in length. The PIN domain was named after its identification in the N-nerminus of the PilT protein (PilT N terminus). PIN domains function as nuclease enzymes that cleave single stranded RNA in a sequence dependent manner.[1]

PIN domains contain three nearly invariant acidic residues. Crystal structures show these residues clustered together in the putative active site. In eukaryotes PIN domains are found in proteins involved in nonsense mediated mRNA decay, in proteins such as SMG5 and SMG6, and in processing of 18S ribosomal RNA. The majority of PIN-domain proteins found in prokaryotes are the toxic components of toxin-antitoxin operon, and toxin-antitoxin gene cassettes, These loci provide a control mechanism that helps free-living prokaryotes cope with nutritional stress.[2]

References

  1. ^ Arcus VL, McKenzie JL, Robson J, Cook GM (2011). "The PIN-domain ribonucleases and the prokaryotic VapBC toxin-antitoxin array". Protein Eng. Des. Sel. 24 (1–2): 33–40. doi:10.1093/protein/gzq081. PMID 21036780. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  2. ^ Gerdes K, Christensen SK, Løbner-Olesen A (2005). "Prokaryotic toxin-antitoxin stress response loci". Nat. Rev. Microbiol. 3 (5): 371–82. doi:10.1038/nrmicro1147. PMID 15864262. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)