 |
PDBsum entry 1ga2
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
|
|
|
|
|
|
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.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
|
J Bacteriol
185:4127-4135
(2003)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
X-Ray crystal structure of the multidomain endoglucanase Cel9G from Clostridium cellulolyticum complexed with natural and synthetic cello-oligosaccharides.
|
|
D.Mandelman,
A.Belaich,
J.P.Belaich,
N.Aghajari,
H.Driguez,
R.Haser.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
Complete cellulose degradation is the first step in the use of biomass as a
source of renewable energy. To this end, the engineering of novel cellulase
activity, the activity responsible for the hydrolysis of the beta-1,4-glycosidic
bonds in cellulose, is a topic of great interest. The high-resolution X-ray
crystal structure of a multidomain endoglucanase from Clostridium cellulolyticum
has been determined at a 1.6-A resolution. The endoglucanase, Cel9G, is
comprised of a family 9 catalytic domain attached to a family III(c)
cellulose-binding domain. The two domains together form a flat platform onto
which crystalline cellulose is suggested to bind and be fed into the active-site
cleft for endolytic hydrolysis. To further dissect the structural basis of
cellulose binding and hydrolysis, the structures of Cel9G in the presence of
cellobiose, cellotriose, and a DP-10 thio-oligosaccharide inhibitor were
resolved at resolutions of 1.7, 1.8, and 1.9 A, respectively.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
|
| |
PubMed id
|
|
Reference
|
|
|
|
|
|
Y.Honda,
N.Shimaya,
K.Ishisaki,
M.Ebihara,
and
H.Taniguchi
(2011).
Elucidation of exo-{beta}-D-glucosaminidase activity of a family 9 glycoside hydrolase (PBPRA0520) from Photobacterium profundum SS9.
|
| |
Glycobiology,
21,
503-511.
|
|
|
|
|
|
|
N.M.Koropatkin,
and
T.J.Smith
(2010).
SusG: a unique cell-membrane-associated alpha-amylase from a prominent human gut symbiont targets complex starch molecules.
|
| |
Structure,
18,
200-215.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
F.Mingardon,
A.Chanal,
C.Tardif,
E.A.Bayer,
and
H.P.Fierobe
(2007).
Exploration of new geometries in cellulosome-like chimeras.
|
| |
Appl Environ Microbiol,
73,
7138-7149.
|
|
|
|
|
|
|
J.C.Blouzard,
C.Bourgeois,
P.de Philip,
O.Valette,
A.Bélaïch,
C.Tardif,
J.P.Bélaïch,
and
S.Pagès
(2007).
Enzyme diversity of the cellulolytic system produced by Clostridium cellulolyticum explored by two-dimensional analysis: identification of seven genes encoding new dockerin-containing proteins.
|
| |
J Bacteriol,
189,
2300-2309.
|
|
|
|
|
|
|
M.Desvaux
(2006).
Unravelling carbon metabolism in anaerobic cellulolytic bacteria.
|
| |
Biotechnol Prog,
22,
1229-1238.
|
|
|
|
|
|
|
V.L.Yip,
and
S.G.Withers
(2006).
Family 4 glycosidases carry out efficient hydrolysis of thioglycosides by an alpha,beta-elimination mechanism.
|
| |
Angew Chem Int Ed Engl,
45,
6179-6182.
|
|
|
|
|
|
|
M.Desvaux
(2005).
Clostridium cellulolyticum: model organism of mesophilic cellulolytic clostridia.
|
| |
FEMS Microbiol Rev,
29,
741-764.
|
|
|
|
|
|
|
L.Hildén,
and
G.Johansson
(2004).
Recent developments on cellulases and carbohydrate-binding modules with cellulose affinity.
|
| |
Biotechnol Lett,
26,
1683-1693.
|
|
|
|
|
|
The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
|
|
Links
