Protein Family Models

This is the C-terminal domain of BclA (Bacillus collagen-like protein of anthracis) which is expressed on spores of Bacillus species. Trimers of the C-terminal domain (CTD) form the tips of the spore's hair-like nap and are the immunodominant target of vertebrate antibodies and drive trimerization [1]. Structure analysis indicate the C-terminal region of the peptide folding into an all-beta structure with a jelly-fold topology, similar to the first human complement C1q, a member of the tumor necrosis factor (TNF)-like family. The C-terminal globular domain has been shown to be located on the exterior of the exosporium, and therefore is critical in determining the immunogenicity of the spore in a mammalian host [2]. [1]. 22405006. Variable lymphocyte receptor recognition of the immunodominant glycoprotein of Bacillus anthracis spores. Kirchdoerfer RN, Herrin BR, Han BW, Turnbough CL Jr, Cooper MD, Wilson IA;. Structure. 2012;20:479-486. [2]. 17879302. Construction, crystal structure and application of a recombinant protein that lacks the collagen-like region of BclA from Bacillus anthracis spores. Liu CQ, Nuttall SD, Tran H, Wilkins M, Streltsov VA, Alderton MR;. Biotechnol Bioeng. 2008;99:774-782. (from Pfam)

Date:

2024-11-04

The D1 accessory domain, also called the stalk domain, is variably present at the N-terminus of copper amine oxidases, and less commonly, glycosyltransferases, cell wall-degrading enzymes, etc. The stalk domain may assist in dimerization.

Date:

2024-10-16

Members of this family belong to the collagen superfamily [1]. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins [2,3]. [1]. 8240831. New members of the collagen superfamily. Mayne R, Brewton RG;. Curr Opin Cell Biol 1993;5:883-890. [2]. 11158359. Streptococcus pyogenes sclB encodes a putative hypervariable surface protein with a collagen-like repetitive structure. Whatmore AM;. Microbiology. 2001;147:419-429. [3]. 21726633. Characterisation of a large family of polymorphic collagen-like proteins in the endospore-forming bacterium Pasteuria ramosa. McElroy K, Mouton L, Du Pasquier L, Qi W, Ebert D;. Res Microbiol. 2011;162:701-714. (from Pfam)

Date:

2024-10-16