View source for 6kge


==Crystal structure of CaDoc0917(R16D)-CaCohA2 complex at pH 5.5==
<StructureSection load='6kge' size='340' side='right'caption='[[6kge]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6kge]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_acetobutylicum_ATCC_824 Clostridium acetobutylicum ATCC 824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KGE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KGE 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]] 2&#8491;</td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6kge FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kge OCA], [https://pdbe.org/6kge PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kge RCSB], [https://www.ebi.ac.uk/pdbsum/6kge PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kge ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q977Y4_CLOAB Q977Y4_CLOAB] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Many important proteins undergo pH-dependent conformational changes resulting in "on-off" switches for protein function, which are essential for regulation of life processes and have wide application potential. Here, we report a pair of cellulosomal assembly modules, comprising a cohesin and a dockerin from Clostridium acetobutylicum, which interact together following a unique pH-dependent switch between two functional sites rather than on-off states. The two cohesin-binding sites on the dockerin are switched from one to the other at pH 4.8 and 7.5 with a 180 degrees rotation of the bound dockerin. Combined analysis by nuclear magnetic resonance spectroscopy, crystal structure determination, mutagenesis, and isothermal titration calorimetry elucidates the chemical and structural mechanism of the pH-dependent switching of the binding sites. The pH-dependent dual-binding-site switch not only represents an elegant example of biological regulation but also provides a new approach for developing pH-dependent protein devices and biomaterials beyond an on-off switch for biotechnological applications.

Discovery and mechanism of a pH-dependent dual-binding-site switch in the interaction of a pair of protein modules.,Yao X, Chen C, Wang Y, Dong S, Liu YJ, Li Y, Cui Z, Gong W, Perrett S, Yao L, Lamed R, Bayer EA, Cui Q, Feng Y Sci Adv. 2020 Oct 23;6(43). pii: 6/43/eabd7182. doi: 10.1126/sciadv.abd7182., Print 2020 Oct. PMID:33097546<ref>PMID:33097546</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6kge" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Clostridium acetobutylicum ATCC 824]]
[[Category: Large Structures]]
[[Category: Feng Y]]
[[Category: Yao X]]