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4dh2

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Current revision (14:35, 14 March 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4dh2]] is a 4 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=4DH2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DH2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4dh2]] is a 4 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=4DH2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DH2 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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4dh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dh2 OCA], [https://pdbe.org/4dh2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dh2 RCSB], [https://www.ebi.ac.uk/pdbsum/4dh2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dh2 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=4dh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dh2 OCA], [https://pdbe.org/4dh2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dh2 RCSB], [https://www.ebi.ac.uk/pdbsum/4dh2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dh2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/A3DCL1_ACET2 A3DCL1_ACET2]]
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[https://www.uniprot.org/uniprot/A3DCL1_ACET2 A3DCL1_ACET2]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Protein-protein interactions play a pivotal role in a large number of biological processes exemplified by the assembly of the cellulosome. Integration of cellulosomal components occurs through the binding of type I cohesin modules located in a non-catalytic molecular scaffold to type I dockerin modules located at the C terminus of cellulosomal enzymes. The majority of type I dockerins display internal symmetry reflected by the presence of two essentially identical cohesin-binding surfaces. Here we report the crystal structures of two novel Clostridium thermocellum type I cohesin-dockerin complexes (CohOlpC-Doc124A and CohOlpA-Doc918). The data revealed that the two dockerins, Doc918 and Doc124A, are unusual because they lack the structural symmetry required to support a dual binding mode. Thus, in both cases, cohesin recognition is dominated by residues located at positions 11, 12, and 19 of one of the dockerin binding surfaces. The alternative binding mode is not possible (Doc918) or highly limited (Doc124A) because residues that assume the critical interacting positions, when dockerins are reoriented by 180 degrees , make steric clashes with the cohesin. In common with a third dockerin (Doc258) that also presents a single binding mode, Doc124A directs the appended cellulase, Cel124A, to the surface of C. thermocellum and not to cellulosomes because it binds preferentially to type I cohesins located at the cell envelope. Although there are a few exceptions, such as Doc918 described here, these data suggest that there is considerable selective pressure for the evolution of a dual binding mode in type I dockerins that direct enzymes into cellulosomes.
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Novel Clostridium thermocellum Type I Cohesin-Dockerin Complexes Reveal a Single Binding Mode.,Bras JL, Alves VD, Carvalho AL, Najmudin S, Prates JA, Ferreira LM, Bolam DN, Romao MJ, Gilbert HJ, Fontes CM J Biol Chem. 2012 Dec 28;287(53):44394-405. doi: 10.1074/jbc.M112.407700. Epub, 2012 Nov 1. PMID:23118225<ref>PMID:23118225</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 4dh2" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Crystal structure of Coh-OlpC(Cthe_0452)-Doc435(Cthe_0435) complex: A novel type I Cohesin-Dockerin complex from Clostridium thermocellum ATTC 27405

PDB ID 4dh2

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