1aoh: Difference between revisions

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-[[Image:1aoh.gif|left|200px]]<br /><applet load="1aoh" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1aoh, resolution 1.7&Aring;" />
-'''SINGLE COHESIN DOMAIN FROM THE SCAFFOLDING PROTEIN CIPA OF THE CLOSTRIDIUM THERMOCELLUM CELLULOSOME'''<br />
-==Overview==
+==SINGLE COHESIN DOMAIN FROM THE SCAFFOLDING PROTEIN CIPA OF THE CLOSTRIDIUM THERMOCELLUM CELLULOSOME==
-The quaternary organization of the cellulosome, a multi-enzymatic, extracellular complex produced by cellulolytic bacteria, depends on, specific interactions between dockerin domains, double EF-hand subunits, carried by the catalytic components, and cohesin domains, individual, receptor subunits linearly arranged within a non-catalytic scaffolding, polypeptide. Cohesin-dockerin complexes with distinct specificities are, also thought to mediate the attachment of cellulosomes to the cell, membrane.We report here the crystal structure of a single cohesin domain, from the scaffolding protein of Clostridium thermocellum. The cohesin, domain folds into a nine-stranded beta-sandwich with an overall "jelly, roll" topology, similar to that observed in bacterial cellulose-binding, domains. Surface-exposed patches of conserved residues promote extensive, intermolecular contacts in the crystal, and suggest a possible binding, target for the EF-hand pair of the cognate dockerin domain. Comparative, studies of cohesin domains indicate that, in spite of low sequence, similarities and different functional roles, all cohesin domains share a, common nine-stranded beta-barrel fold stabilized by a conserved, hydrophobic core.The formation of stable cohesin-dockerin complexes, requires the presence of Ca2+. However, the structure of the cohesin, domain reported here reveals no obvious Ca2+-binding site, and previous, experiments have failed to detect high affinity binding of Ca2+ to the, unliganded dockerin domain of endoglucanase CelD. Based on structural and, biochemical evidence, we propose a model of the cohesin-dockerin complex, in which the dockerin domain requires complexation with its cohesin, partner for protein stability and high-affinity Ca2+ binding.
+<StructureSection load='1aoh' size='340' side='right'caption='[[1aoh]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1aoh]] is a 2 chain structure with sequence from [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=1AOH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AOH FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1aoh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aoh OCA], [https://pdbe.org/1aoh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aoh RCSB], [https://www.ebi.ac.uk/pdbsum/1aoh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aoh ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ao/1aoh_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1aoh ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-AOH 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=1AOH OCA].
+*[[Cellulosome scaffolding protein 3D structures|Cellulosome scaffolding protein 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-The crystal structure of a type I cohesin domain at 1.7 A resolution., Tavares GA, Beguin P, Alzari PM, J Mol Biol. 1997 Oct 31;273(3):701-13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9402065 9402065]
+[[Category: Acetivibrio thermocellus ATCC 27405]]
-[[Category: Clostridium thermocellum]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Alzari PM]]
-[[Category: Alzari, P.M.]]
+[[Category: Tavares G]]
-[[Category: Tavares, G.]]
-[[Category: b-barrel]]
-[[Category: cellulose degradation]]
-[[Category: cellulosome subunit]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:00:04 2007''