1tyj
From Proteopedia
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| - | [[Image:1tyj.gif|left|200px]] | + | [[Image:1tyj.gif|left|200px]] |
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| - | '''Crystal Structure Analysis of type II Cohesin A11 from Bacteroides cellulosolvens''' | + | {{Structure |
| + | |PDB= 1tyj |SIZE=350|CAPTION= <scene name='initialview01'>1tyj</scene>, resolution 1.60Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> and <scene name='pdbligand=MOH:METHANOL'>MOH</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= CipBc(ScaA) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=35825 Bacteroides cellulosolvens]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure Analysis of type II Cohesin A11 from Bacteroides cellulosolvens''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1TYJ is a [ | + | 1TYJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteroides_cellulosolvens Bacteroides cellulosolvens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TYJ OCA]. |
==Reference== | ==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:[http:// | + | 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: Bacteroides cellulosolvens]] | [[Category: Bacteroides cellulosolvens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: beta sandwich]] | [[Category: beta sandwich]] | ||
[[Category: dockerin-binding module]] | [[Category: dockerin-binding module]] | ||
| - | [[Category: | + | [[Category: flap]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:24:58 2008'' |
Revision as of 12:24, 20 March 2008
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| , resolution 1.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | CipBc(ScaA) (Bacteroides cellulosolvens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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