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Dockerin

FieldValue
SymbolDockerin_1
NameDockerin domain
imagePDB_1daq_EBI.jpg
captionStructure of the Dockerin type I domain from C. thermocellum cellulosome.
PfamPF00404
InterProIPR018242
PROSITEPDOC00416
SCOP1daq
CDDcd14253

Dockerin is a protein domain found in the cellulosome cellular structure of anaerobic bacteria. It is found on many endoglucanase enzymes. The dockerin's binding partner is the cohesin domain, located on the scaffoldin protein. This interaction between the dockerin domains of the enzyme constituents of the cellulosome and the cohesin domains of the scaffoldin protein is essential to the construction of the cellulosome complex. The Dockerin domain has two in-tandem repeats of a non-EF hand calcium binding motif. Each motif is characterized by a loop-helix structure. The three-dimensional structure of dockerin has been determined in solution, as well as in complex with Cohesin.

There are three types of Dockerin domains: I, II and III which bind to Cohesin Type I, Cohesin Type II and Cohesin Type III respectively. A type I dockerin domain is 65-70 residues long. The binding specificity of Type I interaction was well studied by structural and mutagenesis studies. Type II interaction is less well characterized.

References

References

  1. (2001). "Cellulosomal scaffoldin-like proteins from Ruminococcus flavefaciens.". J Bacteriol.
  2. {{SCOP. 63447
  3. (March 2001). "Solution structure of a type I dockerin domain, a novel prokaryotic, extracellular calcium-binding domain". J. Mol. Biol..
  4. (2003). "Cellulosome assembly revealed by the crystal structure of the cohesin-dockerin complex". Proceedings of the National Academy of Sciences.
  5. [[InterPro]]: {{InterPro. IPR016134
  6. (February 2005). "Structural characterization of type II dockerin module from the cellulosome of Clostridium thermocellum: calcium-induced effects on conformation and target recognition". Biochemistry.
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protein-structural-motifs protein-domains
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