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J Struct Biol. 2014 Jun;186(3):451-61. doi: 10.1016/j.jsb.2014.01.003. Epub 2014 Jan 14.

Bacterial collagen-like proteins that form triple-helical structures.

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Department of Biochemistry, Robert Wood Johnson Medical School, Rutgers University, Piscataway, NJ 08854, USA. Electronic address:
Department of Biomedical Engineering, Tufts University, Medford, MA 02155, USA. Electronic address:
CSIRO Materials Science and Engineering, Bayview Avenue, Clayton, VIC 3169, Australia. Electronic address:
Department of Biomedical Engineering, Tufts University, Medford, MA 02155, USA. Electronic address:


A large number of collagen-like proteins have been identified in bacteria during the past 10years, principally from analysis of genome databases. These bacterial collagens share the distinctive Gly-Xaa-Yaa repeating amino acid sequence of animal collagens which underlies their unique triple-helical structure. A number of the bacterial collagens have been expressed in Escherichia coli, and they all adopt a triple-helix conformation. Unlike animal collagens, these bacterial proteins do not contain the post-translationally modified amino acid, hydroxyproline, which is known to stabilize the triple-helix structure and may promote self-assembly. Despite the absence of collagen hydroxylation, the triple-helix structures of the bacterial collagens studied exhibit a high thermal stability of 35-39°C, close to that seen for mammalian collagens. These bacterial collagens are readily produced in large quantities by recombinant methods, either in the original amino acid sequence or in genetically manipulated sequences. This new family of recombinant, easy to modify collagens could provide a novel system for investigating structural and functional motifs in animal collagens and could also form the basis of new biomedical materials with designed structural properties and functions.


Biomedical material; Collagen; Prokaryote; Recombinant expression; Thermal stability; Triple-helix

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