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New page: left|200px<br /><applet load="1qzn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qzn, resolution 1.90Å" /> '''Crystal Structure An...
 
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[[Image:1qzn.jpg|left|200px]]<br /><applet load="1qzn" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1qzn, resolution 1.90&Aring;" />
'''Crystal Structure Analysis of a type II cohesin domain from the cellulosome of Acetivibrio cellulolyticus'''<br />


==Overview==
==Crystal Structure Analysis of a type II cohesin domain from the cellulosome of Acetivibrio cellulolyticus==
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.
<StructureSection load='1qzn' size='340' side='right'caption='[[1qzn]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<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>
1QZN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Acetivibrio_cellulolyticus Acetivibrio cellulolyticus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QZN OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</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=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>
==Reference==
</table>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15808849 15808849]
== Function ==
[https://www.uniprot.org/uniprot/Q7WYN3_9FIRM Q7WYN3_9FIRM]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qz/1qzn_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<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;]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 21:51:41 2007''

Latest revision as of 08:19, 14 February 2024

Crystal Structure Analysis of a type II cohesin domain from the cellulosome of Acetivibrio cellulolyticus

1qzn, resolution 1.90Å

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