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<StructureSection load='1aoh' size='340' side='right'caption='[[1aoh]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='1aoh' size='340' side='right'caption='[[1aoh]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1aoh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"ruminiclostridium_thermocellum"_yutin_and_galperin_2013 "ruminiclostridium thermocellum" yutin and galperin 2013]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1AOH FirstGlance]. <br>
<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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cipA, Cthe_3077 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1515 "Ruminiclostridium thermocellum" Yutin and Galperin 2013])</td></tr>
</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'>[http://proteopedia.org/fgij/fg.htm?mol=1aoh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aoh OCA], [http://pdbe.org/1aoh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1aoh RCSB], [http://www.ebi.ac.uk/pdbsum/1aoh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1aoh ProSAT]</span></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>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CIPA_CLOTH CIPA_CLOTH]] Acts as a scaffolding protein in the cellulosome. It promotes binding of cellulose to the catalytic domains of the cellulolytic enzymes.  
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1aoh ConSurf].
</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>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:9402065<ref>PMID:9402065</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1aoh" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Cellulosome scaffolding protein 3D structures|Cellulosome scaffolding protein 3D structures]]
*[[Cellulosome scaffolding protein 3D structures|Cellulosome scaffolding protein 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ruminiclostridium thermocellum yutin and galperin 2013]]
[[Category: Acetivibrio thermocellus ATCC 27405]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Alzari, P M]]
[[Category: Alzari PM]]
[[Category: Tavares, G]]
[[Category: Tavares G]]
[[Category: B-barrel]]
[[Category: Cellulose degradation]]
[[Category: Cellulosome subunit]]
[[Category: Structural protein]]
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