Biology:PIN domain
| PIN domain | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
 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 | ||||||||||
| |||||||||||
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
- ↑ "The PIN-domain ribonucleases and the prokaryotic VapBC toxin-antitoxin array". Protein Engineering, Design & Selection 24 (1–2): 33–40. January 2011. doi:10.1093/protein/gzq081. PMID 21036780.
- ↑ 2.0 2.1 2.2 "Comprehensive classification of the PIN domain-like superfamily". Nucleic Acids Research 45 (12): 6995–7020. July 2017. doi:10.1093/nar/gkx494. PMID 28575517.
- ↑ "Prokaryotic toxin-antitoxin stress response loci". Nature Reviews. Microbiology 3 (5): 371–82. May 2005. doi:10.1038/nrmicro1147. PMID 15864262.
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