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| [[Image:1qzn.jpg|left|200px]]
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| {{Structure
| | ==Crystal Structure Analysis of a type II cohesin domain from the cellulosome of Acetivibrio cellulolyticus== |
| |PDB= 1qzn |SIZE=350|CAPTION= <scene name='initialview01'>1qzn</scene>, resolution 1.90Å
| | <StructureSection load='1qzn' size='340' side='right'caption='[[1qzn]], [[Resolution|resolution]] 1.90Å' scene=''> |
| |SITE=
| | == Structural highlights == |
| |LIGAND=
| | <table><tr><td colspan='2'>[[1qzn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetivibrio_cellulolyticus Acetivibrio cellulolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QZN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QZN FirstGlance]. <br> |
| |ACTIVITY=
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| |GENE= ScaB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=35830 Acetivibrio cellulolyticus])
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qzn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qzn OCA], [https://pdbe.org/1qzn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qzn RCSB], [https://www.ebi.ac.uk/pdbsum/1qzn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qzn ProSAT]</span></td></tr> |
| }}
| | </table> |
| | | == Function == |
| '''Crystal Structure Analysis of a type II cohesin domain from the cellulosome of Acetivibrio cellulolyticus'''
| | [https://www.uniprot.org/uniprot/Q7WYN3_9FIRM Q7WYN3_9FIRM] |
| | | == Evolutionary Conservation == |
| | | [[Image:Consurf_key_small.gif|200px|right]] |
| ==Overview== | | Check<jmol> |
| 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.
| | <jmolCheckbox> |
| | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qz/1qzn_consurf.spt"</scriptWhenChecked> |
| ==About this Structure== | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| 1QZN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Acetivibrio_cellulolyticus Acetivibrio cellulolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QZN OCA].
| | <text>to colour the structure by Evolutionary Conservation</text> |
| | | </jmolCheckbox> |
| ==Reference== | | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qzn ConSurf]. |
| 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:[http://www.ncbi.nlm.nih.gov/pubmed/15808849 15808849]
| | <div style="clear:both"></div> |
| | __TOC__ |
| | </StructureSection> |
| [[Category: Acetivibrio cellulolyticus]] | | [[Category: Acetivibrio cellulolyticus]] |
| [[Category: Single protein]] | | [[Category: Large Structures]] |
| [[Category: Bayer, E A.]] | | [[Category: Bayer EA]] |
| [[Category: Frolow, F.]] | | [[Category: Frolow F]] |
| [[Category: Lamed, R.]] | | [[Category: Lamed R]] |
| [[Category: Noach, I.]] | | [[Category: Noach I]] |
| [[Category: Qi, X.]] | | [[Category: Qi X]] |
| [[Category: Rosenheck, S.]] | | [[Category: Rosenheck S]] |
| [[Category: Shimon, L J.W.]] | | [[Category: Shimon LJW]] |
| [[Category: keywords: cohesins type ii; cellulosome;]]
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| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:44:59 2008''
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