1anu

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[[Image:1anu.gif|left|200px]]
 
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==COHESIN-2 DOMAIN OF THE CELLULOSOME FROM CLOSTRIDIUM THERMOCELLUM==
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The line below this paragraph, containing "STRUCTURE_1anu", creates the "Structure Box" on the page.
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<StructureSection load='1anu' size='340' side='right'caption='[[1anu]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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or leave the SCENE parameter empty for the default display.
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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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{{STRUCTURE_1anu| PDB=1anu | SCENE= }}
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</table>
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== Function ==
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'''COHESIN-2 DOMAIN OF THE CELLULOSOME FROM 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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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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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<jmolCheckbox>
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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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==About this Structure==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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1ANU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ANU OCA].
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==Reference==
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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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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://www.ncbi.nlm.nih.gov/pubmed/9083107 9083107]
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<div style="clear:both"></div>
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[[Category: Clostridium thermocellum]]
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__TOC__
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[[Category: Single protein]]
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</StructureSection>
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[[Category: Bayer, E A.]]
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[[Category: Acetivibrio thermocellus]]
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[[Category: Frolow, F.]]
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[[Category: Large Structures]]
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[[Category: Lamed, R.]]
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[[Category: Bayer EA]]
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[[Category: Morag, E.]]
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[[Category: Frolow F]]
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[[Category: Shimon, L J.W.]]
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[[Category: Lamed R]]
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[[Category: Shoham, Y.]]
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[[Category: Morag E]]
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[[Category: Yaron, S.]]
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[[Category: Shimon LJW]]
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[[Category: Beta sandwich]]
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[[Category: Shoham Y]]
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[[Category: Cellulose digestion]]
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[[Category: Yaron S]]
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[[Category: Cohesin]]
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[[Category: Scaffolding]]
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[[Category: Thermophile]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:29:24 2008''
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Current revision

COHESIN-2 DOMAIN OF THE CELLULOSOME FROM CLOSTRIDIUM THERMOCELLUM

PDB ID 1anu

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