1qzn

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[[Image:1qzn.jpg|left|200px]]<br /><applet load="1qzn" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1qzn.jpg|left|200px]]
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caption="1qzn, resolution 1.90&Aring;" />
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'''Crystal Structure Analysis of a type II cohesin domain from the cellulosome of Acetivibrio cellulolyticus'''<br />
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{{Structure
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|PDB= 1qzn |SIZE=350|CAPTION= <scene name='initialview01'>1qzn</scene>, resolution 1.90&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE= ScaB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=35830 Acetivibrio cellulolyticus])
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}}
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'''Crystal Structure Analysis of a type II cohesin domain from the cellulosome of Acetivibrio cellulolyticus'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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://oca.weizmann.ac.il/oca-bin/ocashort?id=1QZN OCA].
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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].
==Reference==
==Reference==
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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]
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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]
[[Category: Acetivibrio cellulolyticus]]
[[Category: Acetivibrio cellulolyticus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: keywords: cohesins type ii; cellulosome;]]
[[Category: keywords: cohesins type ii; cellulosome;]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:45:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:44:59 2008''

Revision as of 11:45, 20 March 2008


PDB ID 1qzn

Drag the structure with the mouse to rotate
, resolution 1.90Å
Gene: ScaB (Acetivibrio cellulolyticus)
Coordinates: save as pdb, mmCIF, xml



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


Overview

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.

About this Structure

1QZN is a Single protein structure of sequence from Acetivibrio cellulolyticus. Full crystallographic information is available from OCA.

Reference

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

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