PDBsum entry: 1tyj

Structural protein

PDB id: 1tyj

Contents

Protein chain

170 a.a. *

Ligands

EDO ×5

MOH

Waters ×229

* Residue conservation analysis

PDB id:

1tyj

Name:

Structural protein

Title:

Crystal structure analysis of type ii cohesin a11 from bacteroides cellulosolvens

Structure:

Cellulosomal scaffoldin. Chain: a. Fragment: type-ii cohesin domain 11. Engineered: yes

Source:

Bacteroides cellulosolvens. Organism_taxid: 35825. Gene: cipbc(scaa). Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

Resolution:

1.60Å R-factor: 0.170 R-free: 0.198

Authors:

I.Noach,F.Frolow,H.Jakoby,S.Rosenheck,L.J.W.Shimon,R.Lamed, E.A.Bayer

Key ref:

I.Noach et al. (2005). Crystal structure of a type-II cohesin module from the Bacteroides cellulosolvens cellulosome reveals novel and distinctive secondary structural elements. J Mol Biol, 348, 1. PubMed id: 15808849 DOI: 10.1016/j.jmb.2005.02.024

Date:

08-Jul-04 Release date: 26-Apr-05

Protein chain

Q9FDJ9  (Q9FDJ9_9FIRM) -  Cellulosomal scaffoldin (Precursor)

Seq: 2319 a.a.

Struc: 170 a.a.

 Gene Ontology (GO) functional annotation 

• Cellular component: peptidoglycan-based cell wall (1 term)
• Biological process: polysaccharide catabolic process (1 term)
• Biochemical function: carbohydrate binding (1 term)

DOI no: 10.1016/j.jmb.2005.02.024

J Mol Biol 348:1 (2005)

PubMed id: 15808849

Crystal structure of a type-II cohesin module from the Bacteroides cellulosolvens cellulosome reveals novel and distinctive secondary structural elements.

I.Noach, F.Frolow, H.Jakoby, S.Rosenheck, L.W.Shimon, R.Lamed, E.A.Bayer.

ABSTRACT

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.

Selected figure(s)

Figure 6.
Figure 6. Stereo view showing superimposed C^a traces of Bc-cohesin-II (1TYJ, blue), Ct-cohesin-I (1ANU, red) and Cc-cohesin-I (1G1K, green). Superposition was performed using LSQMAN.46

Figure 8.
Figure 8. Surface representation of the Bc-cohesin-II molecule versus Ct-cohesin-I in frontal (bottom) and bird's-eye (top) views. (a) Bc-cohesin-II. Orange areas designate the protruding portions of the b-flaps and the magenta color indicates the a-helix on the top of the molecule. Strand b5 (colored yellow) forms a raised ridge relative to the homologous strand in the type-I cohesins. (b) The contact and recognition residues on the type-I Ct-cohesin-I surface are presented in the equivalent orientation. The molecule shown is the cohesin derived from the cohesin-dockerin heterodimer (1OHZ) without the dockerin. Amino acid residues involved in direct hydrogen bonding to the dockerin are colored green, hydrophobic residues in the cohesin-dockerin contact surface are colored gray, and amino acid residues which interact with the dockerin molecule via bridging water molecules are colored cyan.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2005, 348, 1-0) copyright 2005.

Figures were selected by an automated process.