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4iu3

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==Cohesin-dockerin -X domain complex from Ruminococcus flavefacience==
==Cohesin-dockerin -X domain complex from Ruminococcus flavefacience==
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<StructureSection load='4iu3' size='340' side='right' caption='[[4iu3]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
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<StructureSection load='4iu3' size='340' side='right'caption='[[4iu3]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4iu3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ruminococcus_flavefaciens Ruminococcus flavefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IU3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IU3 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4iu3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ruminococcus_flavefaciens Ruminococcus flavefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IU3 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 1.97&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4iu2|4iu2]]</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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4iu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4iu3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4iu3 RCSB], [http://www.ebi.ac.uk/pdbsum/4iu3 PDBsum]</span></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=4iu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4iu3 OCA], [https://pdbe.org/4iu3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4iu3 RCSB], [https://www.ebi.ac.uk/pdbsum/4iu3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4iu3 ProSAT]</span></td></tr>
</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/A0AEF6_RUMFL A0AEF6_RUMFL]
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The rumen bacterium Ruminococcus flavefaciens produces a highly organized multienzyme cellulosome complex that plays a key role in the degradation of plant cell wall polysaccharides, notably cellulose. The R. flavefaciens cellulosomal system is anchored to the bacterial cell wall through a relatively small ScaE scaffoldin subunit, which bears a single type-IIIe cohesin responsible for the attachment of two major dockerin-containing scaffoldin proteins: ScaB and the cellulose-binding protein CttA. While ScaB recruits the catalytic machinery onto the complex, CttA mediates attachment of the bacterial substrate via its two putative carbohydrate-binding modules (CBMs). In an effort to understand the structural basis for assembly and cell-surface attachment of the cellulosome in R. flavefaciens, we determined the crystal structure of the high-affinity complex (Kd = 20.83 nM) between the ScaE cohesin module (CohE) and its cognate X-dockerin modular dyad (XDoc) from CttA at 1.97-A resolution. The structure reveals an atypical calcium-binding loop containing a 13-residue insert. The results further pinpoint two charged specificity-related residues on the surface of the cohesin module, which are responsible for specific vs. promiscuous cross-strain binding of the dockerin module. In addition, a combined functional role for the three enigmatic dockerin inserts was established, whereby these extraneous segments serve as structural buttresses that reinforce the stalk-like conformation of the X-module, thus segregating its tethered complement of cellulosomal components from the cell surface. The novel structure of the RfCohE-XDoc complex sheds light on divergent dockerin structure and function and provides insight into the specificity features of the type-IIIe cohesin-dockerin interaction.
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Atypical cohesin-dockerin complex responsible for cell-surface attachment of cellulosomal components: binding fidelity, promiscuity, and structural buttresses.,Salama-Alber O, Jobby MK, Chitayat S, Smith SP, White BA, Shimon LJ, Lamed R, Frolow F, Bayer EA J Biol Chem. 2013 Apr 11. PMID:23580648<ref>PMID:23580648</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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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Ruminococcus flavefaciens]]
[[Category: Ruminococcus flavefaciens]]
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[[Category: Bayer, E]]
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[[Category: Bayer E]]
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[[Category: Frolow, F]]
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[[Category: Frolow F]]
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[[Category: Salama-Alber, O]]
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[[Category: Salama-Alber O]]
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[[Category: Beta sandwich]]
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[[Category: Cellulose degradation]]
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[[Category: Structural protein]]
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Current revision

Cohesin-dockerin -X domain complex from Ruminococcus flavefacience

PDB ID 4iu3

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