1qzn
From Proteopedia
(New page: 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=" | + | [[Image:1qzn.jpg|left|200px]]<br /><applet load="1qzn" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qzn, resolution 1.90Å" /> | caption="1qzn, resolution 1.90Å" /> | ||
'''Crystal Structure Analysis of a type II cohesin domain from the cellulosome of Acetivibrio cellulolyticus'''<br /> | '''Crystal Structure Analysis of a type II cohesin domain from the cellulosome of Acetivibrio cellulolyticus'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The incorporation of enzymes into the multi-enzyme cellulosome complex and | + | 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== | ==About this Structure== | ||
| - | 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:// | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: Acetivibrio cellulolyticus]] | [[Category: Acetivibrio cellulolyticus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bayer, E | + | [[Category: Bayer, E A.]] |
[[Category: Frolow, F.]] | [[Category: Frolow, F.]] | ||
[[Category: Lamed, R.]] | [[Category: Lamed, R.]] | ||
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[[Category: Qi, X.]] | [[Category: Qi, X.]] | ||
[[Category: Rosenheck, S.]] | [[Category: Rosenheck, S.]] | ||
| - | [[Category: Shimon, L | + | [[Category: Shimon, L J.W.]] |
[[Category: keywords: cohesins type ii; cellulosome;]] | [[Category: keywords: cohesins type ii; cellulosome;]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:45:29 2008'' |
Revision as of 12:45, 21 February 2008
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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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