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InterPro: IPR016331 Shiga-like toxin, subunit A

Protein matchesHelp
UniProtKB
Matches:
185 proteins
AccessionHelp IPR016331 Shiga-like_toxin_subunit_A
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Contains IPR017988 Ribosome-inactivating protein conserved site
GO Term annotationHelp
Process GO:0017148 negative regulation of translation
Function GO:0030598 rRNA N-glycosylase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This entry represents subunit A of Shiga-like toxin also known as rRNA N-glycosidase; EC:3.2.2.22), which are responsible for inactivation of the ribosome. Shiga-like toxins are produced by Shigella dysenteriae and by bacteriophage that infect Escherichia coli cells [1]. These toxins contain a single A subunit that has N-glycosidase activity and multiple copies of the B subunit that binds to the membrane glycolipid, globotriaosylceramide (Gb3). The A subunit is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits. It catalyses the endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.

Structural linksHelp
SCOP: d.165.1.2
Database linksHelp
Enzyme: EC:3.2.2.22

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR016331 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P09385 Shiga-like toxin 2 subunit A

Q6EH50 Heterotepalin-4

Q9FBI2 Shiga toxin subunit A

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR001574 Ribosome-inactivating protein
IPR017989 Ribosome-inactivating protein subgroup
IPR016331 Shiga-like toxin, subunit A
IPR017988 Ribosome-inactivating protein conserved site
IPR016139 Ribosome-inactivating protein, subdomain 2
IPR016138 Ribosome-inactivating protein, subdomain 1
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp
1. Nakao H, Takeda T.
Escherichia coli Shiga toxin.
9 299-313 2000 [PubMed: 10994531]

Additional ReadingHelp
Fraser ME, Cherney MM, Marcato P, Mulvey GL, Armstrong GD, James MN.
Binding of adenine to Stx2, the protein toxin from Escherichia coli O157:H7.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62 2006 627-30 [PubMed: 16820678]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=16820678&action=stream&blobtype=pdf
Fraser ME, Fujinaga M, Cherney MM, Melton-Celsa AR, Twiddy EM, O'Brien AD, James MN.
Structure of shiga toxin type 2 (Stx2) from Escherichia coli O157:H7.
J. Biol. Chem. 279 2004 27511-7 [PubMed: 15075327]
http://dx.doi.org/10.1074/jbc.M401939200
Fraser ME, Chernaia MM, Kozlov YV, James MN.
Crystal structure of the holotoxin from Shigella dysenteriae at 2.5 A resolution.
Nat. Struct. Biol. 1 1994 59-64 [PubMed: 7656009]
http://dx.doi.org/10.1038/nsb0194-59
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InterPro 23.1