1qzn
From Proteopedia
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'''Crystal Structure Analysis of a type II cohesin domain from the cellulosome of Acetivibrio cellulolyticus''' | '''Crystal Structure Analysis of a type II cohesin domain from the cellulosome of Acetivibrio cellulolyticus''' | ||
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[[Category: Rosenheck, S.]] | [[Category: Rosenheck, S.]] | ||
[[Category: Shimon, L J.W.]] | [[Category: Shimon, L J.W.]] | ||
| - | [[Category: | + | [[Category: Cellulosome;]] |
| - | [[Category: | + | [[Category: Keywords: cohesins type ii]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:53:54 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 03:53, 3 May 2008
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 Page seeded by OCA on Sat May 3 06:53:54 2008
