6kgc: Difference between revisions
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==Crystal structure of CaDoc0917(R49D)-CaCohA2 complex at pH 5.4== | ==Crystal structure of CaDoc0917(R49D)-CaCohA2 complex at pH 5.4== | ||
<StructureSection load='6kgc' size='340' side='right'caption='[[6kgc]]' scene=''> | <StructureSection load='6kgc' size='340' side='right'caption='[[6kgc]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KGC OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6KGC FirstGlance]. <br> | <table><tr><td colspan='2'>[[6kgc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cloab Cloab]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KGC OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6KGC FirstGlance]. <br> | ||
</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=6kgc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kgc OCA], [http://pdbe.org/6kgc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kgc RCSB], [http://www.ebi.ac.uk/pdbsum/6kgc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kgc ProSAT]</span></td></tr> | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6kg8|6kg8]], [[6kg9|6kg9]], [[6kgd|6kgd]], [[6kge|6kge]], [[6kgf|6kgf]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CA_C0910 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272562 CLOAB]), CA_C0917 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272562 CLOAB])</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=6kgc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kgc OCA], [http://pdbe.org/6kgc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kgc RCSB], [http://www.ebi.ac.uk/pdbsum/6kgc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kgc ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6kgc" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Cloab]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Feng Y]] | [[Category: Feng, Y]] | ||
[[Category: Yao X]] | [[Category: Yao, X]] | ||
[[Category: Calcium-binding]] | |||
[[Category: Cellulosome]] | |||
[[Category: Cohesin]] | |||
[[Category: Dockerin]] | |||
[[Category: Hydrolase]] | |||
Revision as of 10:30, 4 November 2020
Crystal structure of CaDoc0917(R49D)-CaCohA2 complex at pH 5.4Crystal structure of CaDoc0917(R49D)-CaCohA2 complex at pH 5.4
Structural highlights
Publication Abstract from PubMedMany 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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