PROSITE documentation PDOC51766 [for PROSITE entry PS51766]

Dockerin domain profile





Description

Plant cell wall polysaccharides comprise the most abundant reservoir of organic carbon in the biosphere. The cellulosomne is a large multienzyme complex used by many anaerobic bacteria for the efficient degradation of plant-cell wall polysaccharides. The principal component of the cellulosome is a scaffoldin subunit, a large enzyme-integrating protein, that contains cohesin modules (usually in multiple copies) for incorporation of the different enzymes and other cellulosomal components. The enzymes contain a complementary type of module, the dockerin domain, that binds tenaciously to the cohesin modules of the scaffoldin subunit [1,2,3,4].

The dockerin domains consist of about 70 amino acid residues and contain two duplicated segments, each of about 22 amino acid residues. The first 12 residues of these duplicated sequences bear remarkable resemblance to the calcium-binding loop of the EF-hand motif (see <PDOC00018>), in which all the calcium-binding residues (i.e., aspartic acids and asparagines) are highly conserved. The second halves of the duplicated sequences appear to form α helices. These helices would be analogous to the F helix of the EF-hand motif [1,2,3,4].

The dockerin domain comprises three α-helices (see <PDB:2MTE>). Helices H1 and H3, which are antiparallel to one another, and the two calcium-binding loops (Ca1 and Ca2) correspond to the tandem duplicated sequences that form the two F-hand motifs. A short loop region and helix H2 connect the F-hand motifs. The 12-residue Ca(2+)-binding loop of each motif coordinates one Ca(2+) ion in the typical pentagonal bipyramid configuration of EF-hand Ca(2+)-binding proteins [3,4].

The profile we developed covers the entire dockerin domain.

Last update:

July 2015 / First entry.

Technical section

PROSITE method (with tools and information) covered by this documentation:

DOCKERIN, PS51766; Dockerin domain profile  (MATRIX)


References

1AuthorsPages S., Belaich A., Belaich J.-P., Morag E., Lamed R., Shoham Y., Bayer E.A.
TitleSpecies-specificity of the cohesin-dockerin interaction between Clostridium thermocellum and Clostridium cellulolyticum: prediction of specificity determinants of the dockerin domain.
SourceProteins 29:517-527(1997).
PubMed ID9408948

2AuthorsBayer E.A., Belaich J.-P., Shoham Y., Lamed R.
TitleThe cellulosomes: multienzyme machines for degradation of plant cell wall polysaccharides.
SourceAnnu. Rev. Microbiol. 58:521-554(2004).
PubMed ID15487947
DOI10.1146/annurev.micro.57.030502.091022

3AuthorsAdams J.J., Pal G., Jia Z., Smith S.P.
TitleMechanism of bacterial cell-surface attachment revealed by the structure of cellulosomal type II cohesin-dockerin complex.
SourceProc. Natl. Acad. Sci. U.S.A. 103:305-310(2006).
PubMed ID16384918
DOI10.1073/pnas.0507109103

4AuthorsChen C., Cui Z., Xiao Y., Cui Q., Smith S.P., Lamed R., Bayer E.A., Feng Y.
TitleRevisiting the NMR solution structure of the Cel48S type-I dockerin module from Clostridium thermocellum reveals a cohesin-primed conformation.
SourceJ. Struct. Biol. 188:188-193(2014).
PubMed ID25270376
DOI10.1016/j.jsb.2014.09.006



PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)