1anu

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(New page: 200px<br /><applet load="1anu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1anu, resolution 2.15&Aring;" /> '''COHESIN-2 DOMAIN OF ...)
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[[Image:1anu.gif|left|200px]]<br /><applet load="1anu" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1anu, resolution 2.15&Aring;" />
 
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'''COHESIN-2 DOMAIN OF THE CELLULOSOME FROM CLOSTRIDIUM THERMOCELLUM'''<br />
 
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==Overview==
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==COHESIN-2 DOMAIN OF THE CELLULOSOME FROM CLOSTRIDIUM THERMOCELLUM==
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BACKGROUND: The scaffoldin component of the cellulolytic bacterium, Clostridium thermocellum is a non-hydrolytic protein which organizes the, hydrolytic enzymes in a large complex, called the cellulosome. Scaffoldin, comprises a series of functional domains, amongst which is a single, cellulose-binding domain and nine cohesin domains which are responsible, for integrating the individual enzymatic subunits into the complex. The, cohesin domains are highly conserved in their primary amino acid, sequences. These domains interact with a complementary domain, termed the, dockerin domain, one of which is located on each enzymatic subunit. The, cohesin-dockerin interaction is the crucial interaction for complex, formation in the cellulosome. The determination of structural information, about the cohesin domain will provide insights into cellulosome assembly, and activity. RESULTS: We have determined the three-dimensional crystal, structure of one of the cohesin domains from C. thermocellum (cohesin 2), at 2.15 A resolution. The domain forms a nine-stranded beta sandwich with, a jelly-roll topology, somewhat similar to the fold displayed by its, neighboring cellulose-binding domain. CONCLUSIONS: The compact nature of, the cohesin structure and its lack of a defined binding pocket suggests, that binding between the cohesin and dockerin domains is characterized by, interactions between exposed surface residues. As the cohesin-dockerin, interaction appears to be rather nonselective, the binding face would, presumably be characterized by surface residues which exhibit both, intraspecies conservation and interspecies dissimilarity. Within the same, species, unconserved surface residues may reflect the position of a given, cohesin domain within the scaffoldin subunit, its orientation and, interactions with neighboring domains.
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<StructureSection load='1anu' size='340' side='right'caption='[[1anu]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1anu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus Acetivibrio thermocellus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ANU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ANU FirstGlance]. <br>
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1ANU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ANU OCA].
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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]] 2.15&#8491;</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=1anu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1anu OCA], [https://pdbe.org/1anu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1anu RCSB], [https://www.ebi.ac.uk/pdbsum/1anu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1anu ProSAT]</span></td></tr>
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==Reference==
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</table>
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A cohesin domain from Clostridium thermocellum: the crystal structure provides new insights into cellulosome assembly., Shimon LJ, Bayer EA, Morag E, Lamed R, Yaron S, Shoham Y, Frolow F, Structure. 1997 Mar 15;5(3):381-90. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9083107 9083107]
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== Function ==
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[[Category: Clostridium thermocellum]]
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[https://www.uniprot.org/uniprot/CIPA_ACET2 CIPA_ACET2] Acts as a scaffolding protein in the cellulosome. It promotes binding of cellulose to the catalytic domains of the cellulolytic enzymes.
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[[Category: Single protein]]
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== Evolutionary Conservation ==
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[[Category: Bayer, E.A.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Frolow, F.]]
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Check<jmol>
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[[Category: Lamed, R.]]
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<jmolCheckbox>
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[[Category: Morag, E.]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/an/1anu_consurf.spt"</scriptWhenChecked>
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[[Category: Shimon, L.J.W.]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: Shoham, Y.]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: Yaron, S.]]
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</jmolCheckbox>
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[[Category: beta sandwich]]
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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=1anu ConSurf].
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[[Category: cellulose digestion]]
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<div style="clear:both"></div>
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[[Category: cohesin]]
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__TOC__
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[[Category: scaffolding]]
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</StructureSection>
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[[Category: thermophile]]
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[[Category: Acetivibrio thermocellus]]
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[[Category: Large Structures]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:59:32 2007''
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[[Category: Bayer EA]]
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[[Category: Frolow F]]
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[[Category: Lamed R]]
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[[Category: Morag E]]
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[[Category: Shimon LJW]]
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[[Category: Shoham Y]]
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[[Category: Yaron S]]

Current revision

COHESIN-2 DOMAIN OF THE CELLULOSOME FROM CLOSTRIDIUM THERMOCELLUM

PDB ID 1anu

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