PDBsum entry: 2jem

Hydrolase

PDB id: 2jem

Contents

Protein chains

232 a.a. *

Waters ×709

* Residue conservation analysis

PDB id:

2jem

Name:

Hydrolase

Title:

Native family 12 xyloglucanase from bacillus licheniformis

Structure:

Endo-beta-1,4-glucanase. Chain: a, b. Synonym: xyloglucanase. Engineered: yes. Mutation: yes

Source:

Bacillus licheniformis. Organism_taxid: 1402. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.78Å R-factor: 0.156 R-free: 0.200

Authors:

T.M.Gloster,F.M.Ibatullin,K.Macauley,J.M.Eklof,S.Roberts, J.P.Turkenburg,M.E.Bjornvad,P.L.Jorgensen,S.Danielsen, K.S.Johansen,T.V.Borchert,K.S.Wilson,H.Brumer,G.J.Davies

Key ref:

T.M.Gloster et al. (2007). Characterization and three-dimensional structures of two distinct bacterial xyloglucanases from families GH5 and GH12. J Biol Chem, 282, 19177-19189. PubMed id: 17376777 DOI: 10.1074/jbc.M700224200

Date:

18-Jan-07 Release date: 20-Mar-07

Protein chains

Q7X4S4  (Q7X4S4_BACLI) -  Endo-beta-1,4-glucanase

Seq: 261 a.a.

Struc: 232 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.3.2.1.4 - Cellulase.
• Reaction: Endohydrolysis of 1,4-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

 Gene Ontology (GO) functional annotation 

• Biological process: metabolic process (2 terms)
• Biochemical function: hydrolase activity (4 terms)

DOI no: 10.1074/jbc.M700224200

J Biol Chem 282:19177-19189 (2007)

PubMed id: 17376777

Characterization and three-dimensional structures of two distinct bacterial xyloglucanases from families GH5 and GH12.

T.M.Gloster, F.M.Ibatullin, K.Macauley, J.M.Eklöf, S.Roberts, J.P.Turkenburg, M.E.Bjørnvad, P.L.Jørgensen, S.Danielsen, K.S.Johansen, T.V.Borchert, K.S.Wilson, H.Brumer, G.J.Davies.

ABSTRACT

The plant cell wall is a complex material in which the cellulose microfibrils are embedded within a mesh of other polysaccharides, some of which are loosely termed "hemicellulose." One such hemicellulose is xyloglucan, which displays a beta-1,4-linked d-glucose backbone substituted with xylose, galactose, and occasionally fucose moieties. Both xyloglucan and the enzymes responsible for its modification and degradation are finding increasing prominence, reflecting both the drive for enzymatic biomass conversion, their role in detergent applications, and the utility of modified xyloglucans for cellulose fiber modification. Here we present the enzymatic characterization and three-dimensional structures in ligand-free and xyloglucan-oligosaccharide complexed forms of two distinct xyloglucanases from glycoside hydrolase families GH5 and GH12. The enzymes, Paenibacillus pabuli XG5 and Bacillus licheniformis XG12, both display open active center grooves grafted upon their respective (beta/alpha)(8) and beta-jelly roll folds, in which the side chain decorations of xyloglucan may be accommodated. For the beta-jelly roll enzyme topology of GH12, binding of xylosyl and pendant galactosyl moieties is tolerated, but the enzyme is similarly competent in the degradation of unbranched glucans. In the case of the (beta/alpha)(8) GH5 enzyme, kinetically productive interactions are made with both xylose and galactose substituents, as reflected in both a high specific activity on xyloglucan and the kinetics of a series of aryl glycosides. The differential strategies for the accommodation of the side chains of xyloglucan presumably facilitate the action of these microbial hydrolases in milieus where diverse and differently substituted substrates may be encountered.

Selected figure(s)

Figure 6.
FIGURE 6. Schematic diagram of the interactions of PpXG5 with XXLG.

Figure 10.
FIGURE 10. Schematic diagram of the interactions of BlXG12 with XXXG/XX.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2007, 282, 19177-19189) copyright 2007.

Figures were selected by an automated process.