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rdf:type |
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lifeskim:mentions |
umls-concept:C0185023,
umls-concept:C0237497,
umls-concept:C0332307,
umls-concept:C0439855,
umls-concept:C0441712,
umls-concept:C0521009,
umls-concept:C0678594,
umls-concept:C1314972,
umls-concept:C1947904,
umls-concept:C1999228,
umls-concept:C2825781
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pubmed:issue |
2
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pubmed:dateCreated |
2006-1-12
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pubmed:databankReference |
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pubmed:abstractText |
Bacterial cell-surface attachment of macromolecular complexes maintains the microorganism in close proximity to extracellular substrates and allows for optimal uptake of hydrolytic byproducts. The cellulosome is a large multienzyme complex used by many anaerobic bacteria for the efficient degradation of plant cell-wall polysaccharides. The mechanism of cellulosome retention to the bacterial cell surface involves a calcium-mediated protein-protein interaction between the dockerin (Doc) module from the cellulosomal scaffold and a cohesin (Coh) module of cell-surface proteins located within the proteoglycan layer. Here, we report the structure of an ultra-high-affinity (K(a) = 1.44 x 10(10) M(-1)) complex between type II Doc, together with its neighboring X module from the cellulosome scaffold of Clostridium thermocellum, and a type II Coh module associated with the bacterial cell surface. Identification of X module-Doc and X module-Coh contacts reveal roles for the X module in Doc stability and enhanced Coh recognition. This extremely tight interaction involves one face of the Coh and both helices of the Doc and comprises significant hydrophobic character and a complementary extensive hydrogen-bond network. This structure represents a unique mechanism for cell-surface attachment in anaerobic bacteria and provides a rationale for discriminating between type I and type II Coh modules.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-10089316,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-10222271,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-10545093,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-10737938,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-11080455,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-11080456,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-11114499,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-11148206,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-11273698,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-11290750,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-11601609,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-11792842,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-11841200,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-11841201,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-12061722,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-12925809,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-14623971,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-14696386,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-14756552,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-15118324,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-15197390,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-15292269,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-15487947,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-15555941,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-15596428,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-15697243,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-15705576,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-15755956,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-15808849,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-15913653,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-2204424,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-2673026,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-2757186,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-7730277,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-8655483,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-8817076,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-8848832,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-9083107,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-9098047,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-9396791,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-9402065,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-9408948,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-9757107,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-9818257,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16384918-9852002
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
103
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
305-10
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:16384918-Bacterial Proteins,
pubmed-meshheading:16384918-Cell Membrane,
pubmed-meshheading:16384918-Cellulosomes,
pubmed-meshheading:16384918-Clostridium thermocellum,
pubmed-meshheading:16384918-Crystallography, X-Ray,
pubmed-meshheading:16384918-Models, Molecular,
pubmed-meshheading:16384918-Protein Binding,
pubmed-meshheading:16384918-Protein Structure, Quaternary,
pubmed-meshheading:16384918-Protein Structure, Tertiary
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pubmed:year |
2006
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pubmed:articleTitle |
Mechanism of bacterial cell-surface attachment revealed by the structure of cellulosomal type II cohesin-dockerin complex.
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pubmed:affiliation |
Department of Biochemistry and Protein Function Discovery Group, Queen's University, Kingston, ON, Canada K7L 3N6.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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