1tyj
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(New page: 200px<br /><applet load="1tyj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tyj, resolution 1.60Å" /> '''Crystal Structure An...)
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Revision as of 00:51, 25 November 2007
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Crystal Structure Analysis of type II Cohesin A11 from Bacteroides cellulosolvens
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
1TYJ is a Single protein structure of sequence from Bacteroides cellulosolvens with EDO and MOH as ligands. 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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