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| | <StructureSection load='1tyj' size='340' side='right'caption='[[1tyj]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='1tyj' size='340' side='right'caption='[[1tyj]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1tyj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35603 Atcc 35603]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TYJ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1TYJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1tyj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudobacteroides_cellulosolvens Pseudobacteroides cellulosolvens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TYJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TYJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MOH:METHANOL'>MOH</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qzn|1qzn]], [[1anu|1anu]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MOH:METHANOL'>MOH</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CipBc(ScaA) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=35825 ATCC 35603])</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=1tyj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tyj OCA], [https://pdbe.org/1tyj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tyj RCSB], [https://www.ebi.ac.uk/pdbsum/1tyj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tyj ProSAT]</span></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=1tyj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tyj OCA], [http://pdbe.org/1tyj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tyj RCSB], [http://www.ebi.ac.uk/pdbsum/1tyj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tyj ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9FDJ9_9FIRM Q9FDJ9_9FIRM] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 35603]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bayer, E A]] | + | [[Category: Pseudobacteroides cellulosolvens]] |
| - | [[Category: Frolow, F]] | + | [[Category: Bayer EA]] |
| - | [[Category: Jakoby, H]] | + | [[Category: Frolow F]] |
| - | [[Category: Lamed, R]] | + | [[Category: Jakoby H]] |
| - | [[Category: Noach, I]] | + | [[Category: Lamed R]] |
| - | [[Category: Rosenheck, S]] | + | [[Category: Noach I]] |
| - | [[Category: Shimon, L J.W]] | + | [[Category: Rosenheck S]] |
| - | [[Category: Alpha helix]]
| + | [[Category: Shimon LJW]] |
| - | [[Category: Beta sandwich]]
| + | |
| - | [[Category: Dockerin-binding module]]
| + | |
| - | [[Category: Flap]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
Q9FDJ9_9FIRM
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The incorporation of enzymes into the multi-enzyme cellulosome complex and its anchoring to the bacterial cell surface are dictated by a set of binding interactions between two complementary protein modules: the cohesin and the dockerin. In this work, the X-ray crystal structure of a type-II cohesin from scaffoldin A of Bacteroides cellulosolvens has been determined to a resolution of 1.6 angstroms using molecular replacement. The type-II B. cellulosolvens cohesin (Bc-cohesin-II) is the first detailed description of a crystal structure for a type-II cohesin, and its features were compared with the known type-I cohesins from Clostridium thermocellum and Clostridium cellulolyticum (Ct-cohesin-I and Cc-cohesin-I, respectively). The overall jelly-roll topology of the type-II Bc-cohesin is very similar to that observed for the type-I cohesins with three additional secondary structures: an alpha-helix and two "beta-flaps" that disrupt the normal course of a beta-strand. In addition, beta-strand 5 is elevated by approximately 4 angstroms on the surface of the molecule, relative to the type-I Ct and Cc-cohesins. Like its type-I analogue, the hydrophobic/aromatic core of Bc-cohesin-II comprises an upper and lower core, but an additional aromatic patch and conserved tryptophan at the crown of the molecule serves to stabilize the alpha-helix of the type-II cohesin. Comparison of Bc-cohesin-II with the known type-I cohesin-dockerin heterodimer suggests that each of the additional secondary structural elements assumes a flanking position relative to the putative dockerin-binding surface. The raised ridge formed by beta-strand 5 confers additional distinctive topographic features to the proposed binding interface that collectively distinguish between the type-II and type-I cohesins.
Crystal structure of a type-II cohesin module from the Bacteroides cellulosolvens cellulosome reveals novel and distinctive secondary structural elements.,Noach I, Frolow F, Jakoby H, Rosenheck S, Shimon LW, Lamed R, Bayer EA J Mol Biol. 2005 Apr 22;348(1):1-12. PMID:15808849[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Noach I, Frolow F, Jakoby H, Rosenheck S, Shimon LW, Lamed R, Bayer EA. Crystal structure of a type-II cohesin module from the Bacteroides cellulosolvens cellulosome reveals novel and distinctive secondary structural elements. J Mol Biol. 2005 Apr 22;348(1):1-12. PMID:15808849 doi:10.1016/j.jmb.2005.02.024
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