Protein Family Models

This is a family of beta-barrel porin-like outer membrane proteins from enteropathogenic Gram-negative bacteria. Intimins and invasins are virulence factors produced by pathogenic Gram-negative bacteria. They carry C-terminal extracellular passenger domains that are involved in adhesion to host cells and N-terminal beta domains that are embedded in the outer membrane. This family represents the beta-barrel porin-like domain in the outer membrane that can be found in intimins, invasins and some inverse autotransporters [1,2]. [1]. 22658748. Crystal structures of the outer membrane domain of intimin and invasin from enterohemorrhagic E. coli and enteropathogenic Y. pseudotuberculosis. Fairman JW, Dautin N, Wojtowicz D, Liu W, Noinaj N, Barnard TJ, Udho E, Przytycka TM, Cherezov V, Buchanan SK;. Structure. 2012;20:1233-1243. [2]. 25596886. The inverse autotransporter family: intimin, invasin and related proteins. Leo JC, Oberhettinger P, Schutz M, Linke D;. Int J Med Microbiol. 2015;305:276-282. (from Pfam)

Date:

2024-10-16

Members of this family adopt a structure consisting of an immunoglobulin-like beta-sandwich, with seven strands in two beta-sheets, arranged in a Greek-key topology. It forms part of the extracellular region of the protein, which can be expressed as a soluble protein (Inv497) that binds integrins and promotes subsequent uptake by cells when attached to bacteria [1]. [1]. 10514372. Crystal structure of invasin: a bacterial integrin-binding protein. Hamburger ZA, Brown MS, Isberg RR, Bjorkman PJ;. Science. 1999;286:291-295. (from Pfam)

Date:

2024-10-16

This family consists of bacterial domains with an Ig-like fold. Members of this family are found in bacterial surface proteins such as intimins and invasins involved in pathogenicity. (from Pfam)

Date:

2024-08-14