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6kg9

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Current revision (07:35, 1 May 2024) (edit) (undo)
 
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==Solution structure of CaDoc0917 from Clostridium acetobutylicum==
==Solution structure of CaDoc0917 from Clostridium acetobutylicum==
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<StructureSection load='6kg9' size='340' side='right'caption='[[6kg9]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='6kg9' size='340' side='right'caption='[[6kg9]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6kg9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cloab Cloab]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KG9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6KG9 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6kg9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_acetobutylicum_ATCC_824 Clostridium acetobutylicum ATCC 824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KG9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KG9 FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6kg8|6kg8]], [[6kgf|6kgf]], [[6kge|6kge]], [[6kgd|6kgd]], [[6kgc|6kgc]]</td></tr>
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<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>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CA_C0917 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272562 CLOAB])</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=6kg9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kg9 OCA], [https://pdbe.org/6kg9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kg9 RCSB], [https://www.ebi.ac.uk/pdbsum/6kg9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kg9 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6kg9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kg9 OCA], [http://pdbe.org/6kg9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kg9 RCSB], [http://www.ebi.ac.uk/pdbsum/6kg9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kg9 ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q97KK2_CLOAB Q97KK2_CLOAB]
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6kg9" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cloab]]
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[[Category: Clostridium acetobutylicum ATCC 824]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Feng, Y]]
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[[Category: Feng Y]]
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[[Category: Yao, X]]
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[[Category: Yao X]]
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[[Category: Calcium-binding]]
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[[Category: Cellulosome]]
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[[Category: Dockerin]]
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[[Category: Hydrolase]]
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Current revision

Solution structure of CaDoc0917 from Clostridium acetobutylicum

PDB ID 6kg9

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