Part:BBa_K4812021:Experience

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Applications of BBa_K4812021

The striking and extensive collagen-like structure of the putative SclB protein appears unprecedented amongst the prokaryotic proteins characterized to date. The extensive run of GXYn repeats resembles the remarkably regular structure of collagen, where virtually every third residue is glycine. It is thus tempting to speculate that SclB may exist in the same triple-helix conformation as collagen, composed of three protein units wound around each other to form a stiff cable. Attempts to express the protein in Escherichia coli have so far proved unsuccessful, perhaps reflecting the unusual structure of SclB. SclB shows many similarities to SclA, but also to M and M-like proteins of S. pyogenes. Like SclA and M proteins, SclB has a hypervariable N-terminal part.

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