2b59

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(New page: 200px<br /><applet load="2b59" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b59, resolution 2.11&Aring;" /> '''The type II cohesin ...)
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[[Image:2b59.gif|left|200px]]<br /><applet load="2b59" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2b59, resolution 2.11&Aring;" />
 
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'''The type II cohesin dockerin complex'''<br />
 
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==Overview==
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==The type II cohesin dockerin complex==
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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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<StructureSection load='2b59' size='340' side='right'caption='[[2b59]], [[Resolution|resolution]] 2.11&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2b59]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus Acetivibrio thermocellus] and [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus_ATCC_27405 Acetivibrio thermocellus ATCC 27405]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B59 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.11&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2b59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b59 OCA], [https://pdbe.org/2b59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b59 RCSB], [https://www.ebi.ac.uk/pdbsum/2b59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b59 ProSAT], [https://www.topsan.org/Proteins/BSGI/2b59 TOPSAN]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A3DF10_ACET2 A3DF10_ACET2]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b5/2b59_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2b59 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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2B59 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum] and [http://en.wikipedia.org/wiki/Clostridium_thermocellum_atcc_27405 Clostridium thermocellum atcc 27405] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2B59 OCA].
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*[[Cellulosome scaffolding protein 3D structures|Cellulosome scaffolding protein 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Mechanism of bacterial cell-surface attachment revealed by the structure of cellulosomal type II cohesin-dockerin complex., Adams JJ, Pal G, Jia Z, Smith SP, Proc Natl Acad Sci U S A. 2006 Jan 10;103(2):305-10. Epub 2005 Dec 29. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16384918 16384918]
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[[Category: Acetivibrio thermocellus]]
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[[Category: Clostridium thermocellum]]
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[[Category: Acetivibrio thermocellus ATCC 27405]]
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[[Category: Clostridium thermocellum atcc 27405]]
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[[Category: Large Structures]]
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[[Category: Protein complex]]
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[[Category: Adams JJ]]
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[[Category: Adams, J.J.]]
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[[Category: Smith SP]]
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[[Category: BSGI, Montreal-Kingston.Bacterial.Structural.Genomics.Initiative.]]
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[[Category: Smith, S.P.]]
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[[Category: CA]]
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[[Category: bsgi]]
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[[Category: cellulosome]]
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[[Category: ef hand]]
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[[Category: montreal-kingston bacterial structural genomics initiative]]
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[[Category: protein-protein complex]]
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[[Category: structural genomics]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:34:07 2007''
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The type II cohesin dockerin complex

PDB ID 2b59

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