4OM9
X-Ray Crystal Structure of the passenger domain of Plasmid encoded toxin, an Autrotansporter Enterotoxin from enteroaggregative Escherichia coli (EAEC)
Summary for 4OM9
| Entry DOI | 10.2210/pdb4om9/pdb |
| Related | 3SZE |
| Descriptor | Serine protease pet (2 entities in total) |
| Functional Keywords | beta-helix, peptidase, alpha-fodrin, hydrolase, eaec, plasmid encoded toxin(pet) |
| Biological source | Escherichia coli |
| Cellular location | Serine protease pet autotransporter: Periplasm (By similarity). Serine protease pet: Secreted. Serine protease pet translocator: Cell outer membrane; Multi-pass membrane protein (By similarity): O68900 |
| Total number of polymer chains | 1 |
| Total formula weight | 104055.56 |
| Authors | Meza-Aguilar, J.D.,Fromme, P.,Torres-Larios, A.,Mendoza-Hernandez, G.,Hernandez-Chinas, U.,Arreguin-Espinosa de Los Monteros, R.A.,Eslava-Campos, C.A.,Fromme, R. (deposition date: 2014-01-27, release date: 2014-03-12, Last modification date: 2023-09-20) |
| Primary citation | Domingo Meza-Aguilar, J.,Fromme, P.,Torres-Larios, A.,Mendoza-Hernandez, G.,Hernandez-Chinas, U.,Arreguin-Espinosa de Los Monteros, R.A.,Eslava Campos, C.A.,Fromme, R. X-ray crystal structure of the passenger domain of plasmid encoded toxin(Pet), an autotransporter enterotoxin from enteroaggregative Escherichia coli (EAEC). Biochem.Biophys.Res.Commun., 445:439-444, 2014 Cited by PubMed Abstract: Autotransporters (ATs) represent a superfamily of proteins produced by a variety of pathogenic bacteria, which include the pathogenic groups of Escherichia coli (E. coli) associated with gastrointestinal and urinary tract infections. We present the first X-ray structure of the passenger domain from the Plasmid-encoded toxin (Pet) a 100 kDa protein at 2.3 Å resolution which is a cause of acute diarrhea in both developing and industrialized countries. Pet is a cytoskeleton-altering toxin that induces loss of actin stress fibers. While Pet (pdb code: 4OM9) shows only a sequence identity of 50% compared to the closest related protein sequence, extracellular serine protease plasmid (EspP) the structural features of both proteins are conserved. A closer structural look reveals that Pet contains a β-pleaded sheet at the sequence region of residues 181-190, the corresponding structural domain in EspP consists of a coiled loop. Secondary, the Pet passenger domain features a more pronounced beta sheet between residues 135 and 143 compared to the structure of EspP. PubMed: 24530907DOI: 10.1016/j.bbrc.2014.02.016 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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