 |
PDBsum entry 1aiw
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Cellulose degradation
|
PDB id
|
|
|
|
1aiw
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
 |
|
Title
|
 |
Solution structure of the cellulose-Binding domain of the endoglucanase z secreted by erwinia chrysanthemi.
|
 |
|
Authors
|
 |
E.Brun,
F.Moriaud,
P.Gans,
M.J.Blackledge,
F.Barras,
D.Marion.
|
 |
|
Ref.
|
 |
Biochemistry, 1997,
36,
16074-16086.
[DOI no: ]
|
 |
|
PubMed id
|
 |
|
 |
 |
|
Abstract
|
 |
|
Two-dimensional proton nuclear magnetic resonance spectroscopy has been used to
determine the three-dimensional structure of the 62 amino acid C-terminal
cellulose-binding domain (CBD) of the endoglucanase Z (CBDEGZ), secreted by
Erwinia chrysanthemi. An experimental data set comprising 958 interproton
nOe-derived restraints was used to calculate 23 structures. The calculated
structures have an average root-mean-square deviation between Cys4 and Cys61 of
0.91 +/- 0.11 A for backbone atoms and 1.18 +/- 0.12 A for the heavy atoms. The
CBDEGZ exhibits a skiboot shape based mainly on a triple antiparallel beta-sheet
perpendicular to a less-ordered summital loop. Three aromatic rings (Trp18,
Trp43, and Tyr44) are localized on one face of the protein and are exposed to
the solvent in a conformation compatible with a cellulose-binding site. Based on
its original folding, we have been able to relate the CBD sequence to those of
several domains of unknown function occurring in several bacterial chitinases as
well as other proteins. This study also provides a structural basis for
analyzing the secretion-related information specific to the CBDEGZ.
|
 |
|
Secondary reference #1
|
 |
|
Title
|
 |
Overproduction, Purification and characterization of the cellulose-Binding domain of the erwinia chrysanthemi secreted endoglucanase egz.
|
 |
|
Authors
|
 |
E.Brun,
P.Gans,
D.Marion,
F.Barras.
|
 |
|
Ref.
|
 |
Eur J Biochem, 1995,
231,
142-148.
|
 |
|
PubMed id
|
 |
|
 |
 |
|
|
 |
|
Secondary reference #2
|
 |
|
Title
|
 |
Periplasmic disulphide bond formation is essential for cellulase secretion by the plant pathogen erwinia chrysanthemi.
|
 |
|
Authors
|
 |
I.Bortoli-German,
E.Brun,
B.Py,
M.Chippaux,
F.Barras.
|
 |
|
Ref.
|
 |
Mol Microbiol, 1994,
11,
545-553.
|
 |
|
PubMed id
|
 |
|
 |
 |
|
|
 |
|
Secondary reference #3
|
 |
|
Title
|
 |
Cellulase egz of erwinia chrysanthemi: structural organization and importance of his98 and glu133 residues for catalysis.
|
 |
|
Authors
|
 |
B.Py,
I.Bortoli-German,
J.Haiech,
M.Chippaux,
F.Barras.
|
 |
|
Ref.
|
 |
Protein Eng, 1991,
4,
325-333.
|
 |
|
PubMed id
|
 |
|
 |
 |
|
|
 |
|
|
|
|
 |