Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2JH2

X-ray crystal structure of a cohesin-like module from Clostridium perfringens

Summary for 2JH2
Entry DOI10.2210/pdb2jh2/pdb
Related2CBI 2CBJ 2J1A 2J1E 2J62 2J7M
DescriptorO-GLCNACASE NAGJ (2 entities in total)
Functional Keywordshydrolase, glycosidase
Biological sourceCLOSTRIDIUM PERFRINGENS
Total number of polymer chains3
Total formula weight46662.49
Authors
Chitayat, S.,Gregg, K.,Adams, J.J.,Ficko-Blean, E.,Bayer, E.A.,Boraston, A.B.,Smith, S.P. (deposition date: 2007-02-19, release date: 2007-11-06, Last modification date: 2024-05-08)
Primary citationChitayat, S.,Gregg, K.,Adams, J.J.,Ficko-Blean, E.,Bayer, E.A.,Boraston, A.B.,Smith, S.P.
Three-Dimensional Structure of a Putative Non- Cellulosomal Cohesin Module from a Clostridium Perfringens Family 84 Glycoside Hydrolase.
J.Mol.Biol., 375:20-, 2008
Cited by
PubMed Abstract: The genomes of myonecrotic strains of Clostridium perfringens encode a large number of secreted glycoside hydrolases. The activities of these enzymes are consistent with degradation of the mucosal layer of the human gastrointestinal tract, glycosaminoglycans and other cellular glycans found throughout the body. In many cases this is thought to aid in the propagation of the major toxins produced by C. perfringens. One such example is the family 84 glycoside hydrolases, which contains five C. perfringens members (CpGH84A-E), each displaying a unique modular architecture. The smallest and most extensively studied member, CpGH84C, comprises an N-terminal catalytic domain with beta-N-acetylglucosaminidase activity, a family 32 carbohydrate-binding module, a family 82 X-module (X82) of unknown function, and a fibronectin type-III-like module. Here we present the structure of the X82 module from CpGH84C, determined by both NMR spectroscopy and X-ray crystallography. CpGH84C X82 adopts a jell-roll fold comprising two beta-sheets formed by nine beta-strands. CpGH84C X82 displays distant amino acid sequence identity yet close structural similarity to the cohesin modules of cellulolytic anaerobic bacteria. Cohesin modules are responsible for the assembly of numerous hydrolytic enzymes in a cellulose-degrading multi-enzyme complex, termed the cellulosome, through a high-affinity interaction with the calcium-binding dockerin module. A planar surface is located on the face of the CpGH84 X82 structure that corresponds to the dockerin-binding region of cellulolytic cohesin modules and has the approximate dimensions to accommodate a dockerin module. The presence of cohesin-like X82 modules in glycoside hydrolases of C. perfringens is an indication that the formation of novel X82-dockerin mediated multi-enzyme complexes, with potential roles in pathogenesis, is possible.
PubMed: 17999932
DOI: 10.1016/J.JMB.2007.10.031
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

226707

건을2024-10-30부터공개중

PDB statisticsPDBj update infoContact PDBjnumon