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| - | [[Image:1tyj.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1tyj| PDB=1tyj | SCENE= }} | | {{STRUCTURE_1tyj| PDB=1tyj | SCENE= }} |
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| - | '''Crystal Structure Analysis of type II Cohesin A11 from Bacteroides cellulosolvens'''
| + | ===Crystal Structure Analysis of type II Cohesin A11 from Bacteroides cellulosolvens=== |
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| - | ==Overview==
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| - | 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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_15808849}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15808849 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15808849}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Dockerin-binding module]] | | [[Category: Dockerin-binding module]] |
| | [[Category: Flap]] | | [[Category: Flap]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:31:25 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:06:31 2008'' |
Revision as of 14:06, 27 July 2008
Template:STRUCTURE 1tyj
Crystal Structure Analysis of type II Cohesin A11 from Bacteroides cellulosolvens
Template:ABSTRACT PUBMED 15808849
About this Structure
1TYJ is a Single protein structure of sequence from Bacteroides cellulosolvens. 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 Sun Jul 27 17:06:31 2008
