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Cohesin-dockerin mediated extracellu...

Queen's University (Canada).

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Cohesin-dockerin mediated extracellular assemblies.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Cohesin-dockerin mediated extracellular assemblies./
Author:	Adams, Jarrett John.
Description:	168 p.
Notes:	Source: Dissertation Abstracts International, Volume: 68-08, Section: B, page: 5198.
Contained By:	Dissertation Abstracts International68-08B.
Subject:	Biology, Bioinformatics. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=NR30216
ISBN:	9780494302163

Cohesin-dockerin mediated extracellular assemblies.
Adams, Jarrett John.

Cohesin-dockerin mediated extracellular assemblies. - 168 p.

Source: Dissertation Abstracts International, Volume: 68-08, Section: B, page: 5198.

Thesis (Ph.D.)--Queen's University (Canada), 2007.

Cohesins and dockerins are specialized protein-protein binding modules that assemble extracellular, multi-enzyme complexes in bacteria. The cellulosome is a multi-enzyme complex that efficiently and synergistically degrades plant cell wall polymers. In cellulosomes, cohesin and dockerin modules integrate an intricate series of enzymatic and non-enzymatic subunits. The mutually exclusive specificity of type I and type II cohesin-dockerin interactions allows for spontaneous assembly of these proteins upon secretion. Recent bioinformatic evidence suggests the infectious noncellulolytic bacterium Clostridium perfringens may utilize cohesin-dockerin interactions to form novel extracellular enzyme complexes involved in virulence.

ISBN: 9780494302163Subjects--Topical Terms:

1018415
Biology, Bioinformatics.

Cohesin-dockerin mediated extracellular assemblies.
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100 1 $a Adams, Jarrett John. $3 1029418
245 1 0 $a Cohesin-dockerin mediated extracellular assemblies.
300 $a 168 p.
500 $a Source: Dissertation Abstracts International, Volume: 68-08, Section: B, page: 5198.
502 $a Thesis (Ph.D.)--Queen's University (Canada), 2007.
520 $a Cohesins and dockerins are specialized protein-protein binding modules that assemble extracellular, multi-enzyme complexes in bacteria. The cellulosome is a multi-enzyme complex that efficiently and synergistically degrades plant cell wall polymers. In cellulosomes, cohesin and dockerin modules integrate an intricate series of enzymatic and non-enzymatic subunits. The mutually exclusive specificity of type I and type II cohesin-dockerin interactions allows for spontaneous assembly of these proteins upon secretion. Recent bioinformatic evidence suggests the infectious noncellulolytic bacterium Clostridium perfringens may utilize cohesin-dockerin interactions to form novel extracellular enzyme complexes involved in virulence.
520 $a In this study, the calcium binding and structural properties of the scaffold and cell surface subunits of Clostridium thermocellum were investigated. Calcium induced a conformational change in the type II dockerin that stabilized a helical interface for protein-protein interactions. Structural analysis of the type II cohesin-dockerin interface identified the novel type II binding orientation and extensively hydrophobic interface chemistry, which was critical for type I-II cohesin-dockerin specificity. The X module of unknown function was shown to augment the type II dockerin affinity through an extensive X-type II dockerin modular interaction and hydrogen bond contacts in the interface. The crystal structures of the heterodimeric complex and the heterotrimeric complex showed an extensive cohesin-X module crystallographic interface. Intertwined cellulosome scaffold subunit associations were stabilized by two extensive and reciprocal CohI-X intermolecular interfaces. Evidence of this association in solution was identified using sedimentation velocity experiments. This is the first polycellulosome crystallographic interface that was not disrupted by dockerin binding.
520 $a This study also identified a group of glycoside bydrolases that form paired enzyme complexes in C. perfringens. Nine novel Coh-Doc pairs were identified that showed promiscuous specificities but ultra-high affinities. The C-terminal cohesin-fibronectin III modular pair and the fivar-dockerin pair from family 84 glycoside hydrolase isoforms were structurally characterized to illustrate these interactions. The C. perfringens Doc module bound in a novel orientation rotated 180° in the 8-3-6-5 plane compared to the C. thermocellum complexes. This was the first characterization of a noncellulolytic Coh-Doc system and the first evidence of glycoside hydrolase assemblies in C. perfringens, including the sialidase and hyaluronidase minor toxins, suggesting synergy.
590 $a School code: 0283.
650 4 $a Biology, Bioinformatics. $3 1018415
650 4 $a Chemistry, Biochemistry. $3 1017722
690 $a 0487
690 $a 0715
710 2 $a Queen's University (Canada). $3 1017786
773 0 $t Dissertation Abstracts International $g 68-08B.
790 $a 0283
791 $a Ph.D.
792 $a 2007
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=NR30216