Rtant part in biofilm formation by targeting EDAcontaining cellular fibronectin (OliverKozup HA et al. 2011; 2013). An extremely diverse role seems for the two collagen like proteins, BclA and BclB, found within the pathogenic bacteria Bacillus anthracis (Sylvestre et al. 2002; Waller et al. 2005). These glycosylated proteins are structural components of the Bacillus exosporium and happen to be shown to become present in thin hairlike surface filaments. Related to Scl1 and Scl2, the central part of BclA and BclB could be the collagenous area using a (GlyXaaYaa)n sequence (Boydston et al. 2005). The length from the central collagenous domain is very polymorphic, with 1791 GlyXaaYaa tripeptides, and the variation of exosporium filament hair length is dependent on the length of BclA collagenous domain (Sylvestre et al.117565-57-8 web 2003). A globular Cterminal domain is located at the distal end from the filaments and types a rugged permeability barrier or shield about the spore (Boydston et al. 2005). Even systems which have only been partly characterized hint in the complexities of quaternary structure, interactions and function that may perhaps be involved with bacterial collagenlike proteins. As an example, collagenlike sequences have already been found as part of the spore appendages of Clostridium taeniosporum (Walker et al. 2007). Two in the 4 appendage proteins have collagenlike sequences: GP85 has 53 GlyXaaYaa repeats, while CL2 has 43 GlyXaaYaa repeats (Walker et al.Fmoc-Ile-OH custom synthesis 2007).PMID:28739548 In other species, like B. anthracis (Steichen et al. 2003), an external nap has been related with triple helical collagen, so this could also prove to become the case for C. taeniosporum, however the formation of triple helical structure has notJ Struct Biol. Author manuscript; available in PMC 2015 June 01.NIHPA Author Manuscript NIHPA Author Manuscript NIHPA Author ManuscriptYu et al.Pageyet been shown. One more partly characterized program could be the collagen like domains reported in Pasteuria ramosa (Mouton et al. 2009; McElroy et al. 2011), where a triplehelical structures has been inferred by comparison towards the Bacillus structure (Mouton et al. 2009; McElroy et al. 2011). Recent research (McElroy et al. 2011), utilizing evaluation of an incomplete genome analysis for P. ramosa, have recommended big complexity for the collagens in this species. The bacterial collagens are frequently related together with the outer membrane in the organisms. In mammalian systems you will find also certain collagens, one example is kinds XIII, XVII, XXIII and XXV that are transmembrane collagens (Franzke et al. 2005; RicardBlum, 2011). The ectodomains of mammalian transmembrane collagens and specific bacterial collagens both show cell adhesive properties. The mammalian collagens are all type II transmembrane proteins, using a short cytosolic Nterminal plus a longer Cterminal ectodomain such as numerous triplehelical domains. The orientation is more variable among bacterial collagens. As an example, the B. anthracis collagenlike proteins having a Cterminal triplehelix domain and globular domain extending out as hairlike filaments, and the S. pyogenes collagenlike proteins have an Nterminal globular domain and triplehelix extending outside on the cell wall.NIHPA Author Manuscript NIHPA Author Manuscript NIHPA Author Manuscript3. Bacterial collagens which can be known to type a triple helix structureDespite the huge number of putative collagen structures in bacteria, only eight have been confirmed as having a triple helical structure. The eight proteins all consis.