Biology:Dockerin
| Dockerin domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Structure of the Dockerin type I domain from C. thermocellum cellulosome. | |||||||||
| Identifiers | |||||||||
| Symbol | Dockerin_1 | ||||||||
| Pfam | PF00404 | ||||||||
| InterPro | IPR018242 | ||||||||
| PROSITE | PDOC00416 | ||||||||
| SCOP2 | 1daq / SCOPe / SUPFAM | ||||||||
| CDD | cd14253 | ||||||||
| |||||||||
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.[1] 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.[2] The three-dimensional structure of dockerin has been determined in solution,[3] as well as in complex with Cohesin.[4]
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.[5] The binding specificity of Type I interaction was well studied by structural and mutagenesis studies. Type II interaction is less well characterized.[6]
See also
- EF hand
- cellulosome
References
- ↑ "Cellulosomal scaffoldin-like proteins from Ruminococcus flavefaciens.". J Bacteriol 183 (6): 1945–53. 2001. doi:10.1128/JB.183.6.1945-1953.2001. PMID 11222592.
- ↑ SCOP 63447
- ↑ PDB: 1DAQ; "Solution structure of a type I dockerin domain, a novel prokaryotic, extracellular calcium-binding domain". J. Mol. Biol. 307 (3): 745–53. March 2001. doi:10.1006/jmbi.2001.4522. PMID 11273698.
- ↑ PDB: 1OHZ; Carvalho, A. L.; Dias, F. M. V.; Prates, J. A. M.; Nagy, T.; Gilbert, H. J.; Davies, G. J.; Ferreira, L. M. A.; Romao, M. J. et al. (2003). "Cellulosome assembly revealed by the crystal structure of the cohesin-dockerin complex". Proceedings of the National Academy of Sciences 100 (24): 13809–13814. doi:10.1073/pnas.1936124100. PMID 14623971.
- ↑ InterPro: InterPro: IPR016134
- ↑ "Structural characterization of type II dockerin module from the cellulosome of Clostridium thermocellum: calcium-induced effects on conformation and target recognition". Biochemistry 44 (6): 2173–82. February 2005. doi:10.1021/bi048039u. PMID 15697243.
External links
Protein Structure:
- "Solution structure of a type I dockerin domain, a novel prokaryotic, extracellular calcium-binding domain". J Mol Biol 307 (3): 745–753. 2001. doi:10.1006/jmbi.2001.4522. PMID 11273698.
- "Cellulosomes-structure and ultrastructure". J Struct Biol 124 (2–3): 221–234. 1998. doi:10.1006/jsbi.1998.4065. PMID 10049808.
Specificity Characterization:
- "Cohesin-dockerin microarray: Diverse specificities between two complementary families of interacting protein modules". Proteomics 8 (5): 968–979. 2008. doi:10.1002/pmic.200700486. PMID 18219699.
- "Structural characterization of type II dockerin module from the cellulosome of Clostridium thermocellum: calcium-induced effects on conformation and target recognition". Biochemistry 44 (6): 2173–2182. 2005. doi:10.1021/bi048039u. PMID 15697243.
- "Cohesin-dockerin interactions within and between Clostridium josui and Clostridium thermocellum: binding selectivity between cognate dockerin and cohesin domains and species specificity". J Biol Chem 279 (11): 9867–9874. 2004. doi:10.1074/jbc.M308673200. PMID 14688277.
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