 |
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
 |
|
 |
|
 |
|
|
Gene Ontology (GO) functional annotation
|
|
|
|
 |
 |
 |
|
 |
 |
 |
 |
|
 |
|
Biological process
|
carbohydrate metabolic process
|
1 term
|
 |
|
Biochemical function
|
hydrolase activity, hydrolyzing O-glycosyl compounds
|
1 term
|
 |
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
| |
|
DOI no:
|
Febs J
276:1048-1058
(2009)
|
|
PubMed id:
|
|
|
|
|
| |
|
Crystal structure of a family 16 endoglucanase from the hyperthermophile Pyrococcus furiosus- structural basis of substrate recognition.
|
|
A.Ilari,
A.Fiorillo,
S.Angelaccio,
R.Florio,
R.Chiaraluce,
J.van der Oost,
V.Consalvi.
|
|
|
|
| |
ABSTRACT
|
|
|
| |
|
Bacterial and archaeal endo-beta-1,3-glucanases that belong to glycoside
hydrolase family 16 share a beta-jelly-roll fold, but differ significantly in
sequence and in substrate specificity. The crystal structure of the laminarinase
(EC 3.2.1.39) from the hyperthermophilic archaeon Pyrococcus furiosus (pfLamA)
has been determined at 2.1 A resolution by molecular replacement. The pfLamA
structure reveals a kink of six residues (72-77) at the entrance of the
catalytic cleft. This peptide is absent in the endoglucanases from alkaliphilic
Nocardiopsis sp. strain F96 and Bacillus macerans, two proteins displaying an
overall fold similar to that of pfLamA, but with different substrate
specificity. A deletion mutant of pfLamA, lacking residues 72-75, hydrolyses the
mixed-linkage beta-1,3-1,4-glucan lichenan 10 times more efficiently than the
wild-type protein, indicating the importance of the kink in substrate preference.
|
|
|
|
|
|
|
 |
 |
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
 |
| |
PubMed id
|
 |
Reference
|
 |
|
|
|
 |
J.Cota,
T.M.Alvarez,
A.P.Citadini,
C.R.Santos,
M.de Oliveira Neto,
R.R.Oliveira,
G.M.Pastore,
R.Ruller,
R.A.Prade,
M.T.Murakami,
and
F.M.Squina
(2011).
Mode of operation and low-resolution structure of a multi-domain and hyperthermophilic endo-β-1,3-glucanase from Thermotoga petrophila.
|
| |
Biochem Biophys Res Commun, 406,
590-594.
|
 |
|
|
|
|
 |
J.Vasur,
R.Kawai,
E.Andersson,
K.Igarashi,
M.Sandgren,
M.Samejima,
and
J.Ståhlberg
(2009).
X-ray crystal structures of Phanerochaete chrysosporium Laminarinase 16A in complex with products from lichenin and laminarin hydrolysis.
|
| |
FEBS J, 276,
3858-3869.
|
 |
|
 |
 |
|
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.
|
|