View source for Dockerin

{{Infobox protein family
| Symbol = Dockerin_1
| Name = Dockerin domain
| image = PDB_1daq_EBI.jpg
| width =
| caption = Structure of the Dockerin type I domain from C. thermocellum cellulosome.
| Pfam = PF00404
| InterPro = IPR018242
| SMART =
| PROSITE = PDOC00416
| SCOP = 1daq
| TCDB = 
| OPM family = 
| OPM protein = 
| CDD = cd14253
| PDB = 
}}

'''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|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.<ref name="pmid11222592">{{cite journal| vauthors=Ding SY, Rincon MT, Lamed R, Martin JC, McCrae SI, Aurilia V| title=Cellulosomal scaffoldin-like proteins from Ruminococcus flavefaciens. | journal=J Bacteriol | year= 2001 | volume= 183 | issue= 6 | pages= 1945–53 | pmid=11222592 | doi=10.1128/JB.183.6.1945-1953.2001 | pmc=95089 |display-authors=etal}}</ref> 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]].<ref>{{SCOP|63447}}</ref>  The three-dimensional structure of dockerin has been determined in solution,<ref name="pmid11273698">{{PDB|1DAQ}}; {{cite journal | vauthors = Lytle BL, Volkman BF, Westler WM, Heckman MP, Wu JH | title = Solution structure of a type I dockerin domain, a novel prokaryotic, extracellular calcium-binding domain | journal = J. Mol. Biol. | volume = 307 | issue = 3 | pages = 745–53 |date=March 2001 | pmid = 11273698 | doi = 10.1006/jmbi.2001.4522 }}</ref> as well as in complex with Cohesin.<ref name="pmid14623971">{{PDB|1OHZ}}; {{cite journal|last1=Carvalho|first1=A. L.|last2=Dias|first2=F. M. V.|last3=Prates|first3=J. A. M.|last4=Nagy|first4=T.|last5=Gilbert|first5=H. J.|author-link5=Harry J. Gilbert|last6=Davies|first6=G. J.|author-link6=Gideon Davies|last7=Ferreira|first7=L. M. A.|last8=Romao|first8=M. J.|last9=Fontes|first9=C. M. G. A.|title=Cellulosome assembly revealed by the crystal structure of the cohesin-dockerin complex|journal=Proceedings of the National Academy of Sciences|volume=100|issue=24|year=2003|pages=13809–13814|doi=10.1073/pnas.1936124100|pmid = 14623971 | pmc = 283503|doi-access=free}}</ref>

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 [[residue (chemistry)|residue]]s long.<ref>[[InterPro]]: {{InterPro|IPR016134}}</ref> The binding specificity of Type I interaction was well studied by structural and [[mutagenesis]] studies. Type II interaction is less well characterized.<ref name="pmid15697243">{{cite journal | vauthors = Adams JJ, Webb BA, Spencer HL, Smith SP | title = Structural characterization of type II dockerin module from the cellulosome of Clostridium thermocellum: calcium-induced effects on conformation and target recognition | journal = Biochemistry | volume = 44 | issue = 6 | pages = 2173–82 |date=February 2005 | pmid = 15697243 | doi = 10.1021/bi048039u }}</ref>

==See also==
*[[EF hand]]
*[[cellulosome]]

==References==
{{reflist}}

==External links==

Protein Structure:
* {{cite journal |vauthors=Lytle BL, Volkman BF, Westler WM, Heckman MP, Wu JH|title=Solution structure of a type I dockerin domain, a novel prokaryotic, extracellular calcium-binding domain|journal=J Mol Biol|volume=307|pages=745–753|year=2001 |pmid=11273698 |doi=10.1006/jmbi.2001.4522 |issue=3 }}
* {{cite journal |vauthors=Bayer EA, Shimon LJ, Shoham Y, Lamed R|title=Cellulosomes-structure and ultrastructure|journal=J Struct Biol|volume=124|issue=2–3|pages=221–234|year=1998|pmid=10049808 |doi=10.1006/jsbi.1998.4065}}

Specificity Characterization:
* {{cite journal |vauthors=Haimovitz R, Barak Y, Morag E, Voronov-Goldman M, Shoham Y, Lamed R, Bayer EA|title=Cohesin-dockerin microarray: Diverse specificities between two complementary families of interacting protein modules|journal=Proteomics|volume=8|issue=5|pages=968–979|year=2008 |pmid=18219699 |doi=10.1002/pmic.200700486|s2cid=206360888}}
* {{cite journal |vauthors=Adams JJ, Webb BA, Spencer HL, Smith SP|title=Structural characterization of type II dockerin module from the cellulosome of Clostridium thermocellum: calcium-induced effects on conformation and target recognition|journal=Biochemistry|volume=44|issue=6|pages=2173–2182 |year=2005 |pmid=15697243 |doi=10.1021/bi048039u}}
* {{cite journal |vauthors=Jindou S, Soda A, Karita S, Kajino T, Béguin P, Wu JH, Inagaki M, Kimura T, Sakka K, Ohmiya K|title=Cohesin-dockerin interactions within and between Clostridium josui and Clostridium thermocellum: binding selectivity between cognate dockerin and cohesin domains and species specificity|journal=J Biol Chem|volume=279|issue=11|pages=9867–9874|year=2004 |pmid=14688277 |doi=10.1074/jbc.M308673200|doi-access=free}}

[[Category:Protein structural motifs]]
[[Category:Protein domains]]