4uyq
From Proteopedia
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| - | ''' | + | ==High resolution structure of the third cohesin ScaC in complex with the ScaB dockerin with a mutation in the C-terminal helix (IN to SI) from Acetivibrio cellulolyticus displaying a type I interaction.== |
| + | <StructureSection load='4uyq' size='340' side='right' caption='[[4uyq]], [[Resolution|resolution]] 1.81Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4uyq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Acetivibrio_cellulolyticus Acetivibrio cellulolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UYQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UYQ FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4uyp|4uyp]], [[4uz8|4uz8]], [[4uzn|4uzn]], [[4uzp|4uzp]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4uyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uyq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uyq RCSB], [http://www.ebi.ac.uk/pdbsum/4uyq PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The cellulosome, a highly elaborate extracellular multi-enzyme complex of cellulases and hemicellulases, is responsible for the efficient degradation of plant cell-wall carbohydrates by anaerobic microorganisms. Cohesin and dockerin recognition pairs are integral to the architecture of the cellulosome. Thus, type I cohesin:dockerins are important for attaching the modular enzymatic components to primary scaffoldins to form the cellulosome. In contrast, type II dockerins located in primary scaffoldins bind to anchoring scaffoldins, thus contributing to the cell-surface attachment of the entire complex. Since anchoring scaffoldins usually contain more than one type II cohesin, they contribute to the assembly of polycellulosomes. Acetivibrio cellulolyticus possesses an extremely complex cellulosome arrangement which is organized by a primary enzyme-binding scaffoldin (ScaA), two anchoring scaffoldins (ScaC and ScaD) and an unusual adaptor scaffoldin (ScaB). A ScaB dockerin mutated to inactivate one of the two putative cohesin-binding interfaces complexed with the ScaC cohesin from A. cellulolyticus has been purified and crystallized and data were collected from tetragonal and monoclinic crystal forms to resolutions of 1.5 and 6.0 A, respectively. | ||
| - | + | Purification, crystallization and preliminary X-ray characterization of the Acetivibrio cellulolyticus type I cohesin ScaC in complex with the ScaB dockerin.,Cameron K, Alves VD, Bule P, Ferreira LM, Fontes CM, Najmudin S Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Sep 1;68(Pt 9):1030-3., doi: 10.1107/S1744309112031922. Epub 2012 Aug 30. PMID:22949188<ref>PMID:22949188</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Acetivibrio cellulolyticus]] | ||
| + | [[Category: Cameron, K]] | ||
| + | [[Category: Fontes, C M.G A]] | ||
[[Category: Najmudin, S]] | [[Category: Najmudin, S]] | ||
| - | [[Category: | + | [[Category: Adaptor scaffoldin scab]] |
| - | [[Category: | + | [[Category: Anchoring scaffolding scac]] |
| + | [[Category: Cell adhesion-protein binding complex]] | ||
| + | [[Category: Cellulosome]] | ||
| + | [[Category: Type 1 cohesin-dockerin intereaction]] | ||
Revision as of 12:49, 15 April 2015
High resolution structure of the third cohesin ScaC in complex with the ScaB dockerin with a mutation in the C-terminal helix (IN to SI) from Acetivibrio cellulolyticus displaying a type I interaction.
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