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In molecular biology the '''PIN domain''' is a [[protein domain]] that is about 130 amino acids in length. PIN domains function as [[nuclease]] enzymes that cleave [[ssRNA|single stranded RNA]] in a sequence- or structure-dependent manner.<ref name="pmid21036780">{{cite journal | vauthors = Arcus VL, McKenzie JL, Robson J, Cook GM | title = The PIN-domain ribonucleases and the prokaryotic VapBC toxin-antitoxin array | journal = Protein Engineering, Design & Selection | volume = 24 | issue = |
In molecular biology the '''PIN domain''' is a [[protein domain]] that is about 130 amino acids in length. PIN domains function as [[nuclease]] enzymes that cleave [[ssRNA|single stranded RNA]] in a sequence- or structure-dependent manner.<ref name="pmid21036780">{{cite journal | vauthors = Arcus VL, McKenzie JL, Robson J, Cook GM | title = The PIN-domain ribonucleases and the prokaryotic VapBC toxin-antitoxin array | journal = Protein Engineering, Design & Selection | volume = 24 | issue = 1–2 | pages = 33–40 | date = January 2011 | pmid = 21036780 | doi = 10.1093/protein/gzq081 | doi-access = free }}</ref><ref name=":0" /> |
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PIN domains contain four nearly invariant acidic residues.<ref name=":0" /> 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]]s.<ref name=":0">{{cite journal | vauthors = Matelska D, Steczkiewicz K, Ginalski K | title = Comprehensive classification of the PIN domain-like superfamily | journal = Nucleic Acids Research | volume = 45 | issue = 12 | pages = 6995–7020 | date = July 2017 | pmid = 28575517 | pmc = 5499597 | doi = 10.1093/nar/gkx494 }}</ref> These loci provide a control mechanism that helps free-living prokaryotes cope with nutritional stress.<ref name="pmid15864262">{{cite journal | vauthors = Gerdes K, Christensen SK, Løbner-Olesen A | title = Prokaryotic toxin-antitoxin stress response loci | journal = Nature Reviews. Microbiology | volume = 3 | issue = 5 | pages = 371–82 | date = May 2005 | pmid = 15864262 | doi = 10.1038/nrmicro1147 }}</ref> |
PIN domains contain four nearly invariant acidic residues.<ref name=":0" /> 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]]s.<ref name=":0">{{cite journal | vauthors = Matelska D, Steczkiewicz K, Ginalski K | title = Comprehensive classification of the PIN domain-like superfamily | journal = Nucleic Acids Research | volume = 45 | issue = 12 | pages = 6995–7020 | date = July 2017 | pmid = 28575517 | pmc = 5499597 | doi = 10.1093/nar/gkx494 }}</ref> These loci provide a control mechanism that helps free-living prokaryotes cope with nutritional stress.<ref name="pmid15864262">{{cite journal | vauthors = Gerdes K, Christensen SK, Løbner-Olesen A | title = Prokaryotic toxin-antitoxin stress response loci | journal = Nature Reviews. Microbiology | volume = 3 | issue = 5 | pages = 371–82 | date = May 2005 | pmid = 15864262 | doi = 10.1038/nrmicro1147 | s2cid = 13417307 }}</ref> |
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== References == |
== References == |
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Latest revision as of 22:02, 11 September 2020
| PIN domain | |||||||||||
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 Crystal structure of PIN (PilT N-terminus) domain (AF0591) from Archaeoglobus fulgidus at 1.90 Angstrom resolution. 1o4w | |||||||||||
| Identifiers | |||||||||||
| Symbol | PIN | ||||||||||
| Pfam | PF01850 | ||||||||||
| InterPro | IPR002716 | ||||||||||
| SMART | CBS | ||||||||||
| SCOP2 | 3dbo / SCOPe / SUPFAM | ||||||||||
| CDD | cd09852 | ||||||||||
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In molecular biology the PIN domain is a protein domain that is about 130 amino acids in length. PIN domains function as nuclease enzymes that cleave single stranded RNA in a sequence- or structure-dependent manner.[1][2]
PIN domains contain four nearly invariant acidic residues.[2] 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 operons.[2] These loci provide a control mechanism that helps free-living prokaryotes cope with nutritional stress.[3]
References
[edit]- ^ Arcus VL, McKenzie JL, Robson J, Cook GM (January 2011). "The PIN-domain ribonucleases and the prokaryotic VapBC toxin-antitoxin array". Protein Engineering, Design & Selection. 24 (1–2): 33–40. doi:10.1093/protein/gzq081. PMID 21036780.
- ^ a b c Matelska D, Steczkiewicz K, Ginalski K (July 2017). "Comprehensive classification of the PIN domain-like superfamily". Nucleic Acids Research. 45 (12): 6995–7020. doi:10.1093/nar/gkx494. PMC 5499597. PMID 28575517.
- ^ Gerdes K, Christensen SK, Løbner-Olesen A (May 2005). "Prokaryotic toxin-antitoxin stress response loci". Nature Reviews. Microbiology. 3 (5): 371–82. doi:10.1038/nrmicro1147. PMID 15864262. S2CID 13417307.