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PDBsum entry 1mac
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Hydrolase (glucanase)
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PDB id
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1mac
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* Residue conservation analysis
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PDB id:
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Hydrolase (glucanase)
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Title:
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Crystal structure and site-directed mutagenesis of bacillus macerans endo-1,3-1,4-beta-glucanase
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Structure:
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1,3-1,4-beta-d-glucan 4-glucanohydrolase. Chain: a, b. Engineered: yes
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Source:
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Paenibacillus macerans. Organism_taxid: 44252. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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Authors:
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M.Hahn,U.Heinemann
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Key ref:
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M.Hahn
et al.
(1995).
Crystal structure and site-directed mutagenesis of Bacillus macerans endo-1,3-1,4-beta-glucanase.
J Biol Chem,
270,
3081-3088.
PubMed id:
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Date:
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22-Dec-94
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Release date:
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27-Feb-95
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PROCHECK
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Headers
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References
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P23904
(GUB_PAEMA) -
Beta-glucanase from Paenibacillus macerans
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Seq: Struc:
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237 a.a.
212 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Enzyme class:
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E.C.3.2.1.73
- licheninase.
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Reaction:
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Hydrolysis of 1,4-beta-D-glycosidic linkages in beta-D-glucans containing 1,3- and 1,4-bonds.
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J Biol Chem
270:3081-3088
(1995)
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PubMed id:
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Crystal structure and site-directed mutagenesis of Bacillus macerans endo-1,3-1,4-beta-glucanase.
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M.Hahn,
O.Olsen,
O.Politz,
R.Borriss,
U.Heinemann.
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ABSTRACT
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In beta-glucans those beta-1,4 glycosidic bonds which are adjacent to beta-1,3
bonds are cleaved by endo-1,3-1,4-beta-glucanases (beta-glucanases). Here, the
relationship between structure and activity of the beta-glucanase of Bacillus
macerans is studied by x-ray crystallography and site-directed mutagenesis of
active site residues. Crystal structure analysis at 2.3-A resolution reveals a
jelly-roll protein structure with a deep active site channel harboring the amino
acid residues Trp101, Glu103, Asp105, and Glu107 as in the hybrid Bacillus
beta-glucanase H(A16-M) (Keitel, T., Simon, O., Borriss, R., and Heinemann, U.
(1993) Proc. Natl. Acad. Sci. U.S.A. 90, 5287-5291). Different mutant proteins
with substitutions in these residues are generated by site-directed mutagenesis,
isolated, and characterized. Compared with the wild-type enzyme their activity
is reduced to less than 1%. Several mutants with isosteric substitutions in
Glu103 and Glu107 are completely inactive, suggesting a direct role of these
residues in glycosyl bond hydrolysis. The kinetic properties of mutant
beta-glucanases and the crystal structure of the wild-type enzyme are consistent
with a mechanism where Glu103 and Glu107 are the catalytic amino acid residues
responsible for cleavage of the beta-1,4 glycosidic bond within the substrate
molecule.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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T.Takeda,
M.Takahashi,
T.Nakanishi-Masuno,
Y.Nakano,
H.Saitoh,
A.Hirabuchi,
S.Fujisawa,
and
R.Terauchi
(2010).
Characterization of endo-1,3-1,4-β-glucanases in GH family 12 from Magnaporthe oryzae.
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Appl Microbiol Biotechnol,
88,
1113-1123.
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B.Mertz,
X.Gu,
and
P.J.Reilly
(2009).
Analysis of functional divergence within two structurally related glycoside hydrolase families.
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Biopolymers,
91,
478-495.
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J.Qiao,
B.Dong,
Y.Li,
B.Zhang,
and
Y.Cao
(2009).
Cloning of a beta-1,3-1,4-glucanase gene from Bacillus subtilis MA139 and its functional expression in Escherichia coli.
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Appl Biochem Biotechnol,
152,
334-342.
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Y.M.Cheng,
T.Y.Hong,
C.C.Liu,
and
M.Meng
(2009).
Cloning and functional characterization of a complex endo-beta-1,3-glucanase from Paenibacillus sp.
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Appl Microbiol Biotechnol,
81,
1051-1061.
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PDB codes:
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M.Yuki,
S.Moriya,
T.Inoue,
and
T.Kudo
(2008).
Transcriptome analysis of the digestive organs of Hodotermopsis sjostedti, a lower termite that hosts mutualistic microorganisms in its hindgut.
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Zoolog Sci,
25,
401-406.
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S.Yang,
Y.Wang,
Z.Jiang,
and
C.Hua
(2008).
Crystallization and preliminary X-ray analysis of a 1,3-1,4-beta-glucanase from Paecilomyces thermophila.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
64,
754-756.
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T.Y.Hong,
Y.Y.Hsiao,
M.Meng,
and
T.T.Li
(2008).
The 1.5 A structure of endo-1,3-beta-glucanase from Streptomyces sioyaensis: evolution of the active-site structure for 1,3-beta-glucan-binding specificity and hydrolysis.
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Acta Crystallogr D Biol Crystallogr,
64,
964-970.
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PDB code:
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C.Deutsch,
and
B.Krishnamoorthy
(2007).
Four-body scoring function for mutagenesis.
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Bioinformatics,
23,
3009-3015.
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D.von Wettstein
(2007).
From analysis of mutants to genetic engineering.
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Annu Rev Plant Biol,
58,
1.
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G.Fibriansah,
S.Masuda,
N.Koizumi,
S.Nakamura,
and
T.Kumasaka
(2007).
The 1.3 A crystal structure of a novel endo-beta-1,3-glucanase of glycoside hydrolase family 16 from alkaliphilic Nocardiopsis sp. strain F96.
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Proteins,
69,
683-690.
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PDB code:
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J.Dong,
Y.Tamaru,
and
T.Araki
(2007).
A unique beta-agarase, AgaA, from a marine bacterium, Vibrio sp. strain PO-303.
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Appl Microbiol Biotechnol,
74,
1248-1255.
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J.Dong,
Y.Tamaru,
and
T.Araki
(2007).
Molecular cloning, expression, and characterization of a beta-agarase gene, agaD, from a marine bacterium, Vibrio sp. strain PO-303.
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Biosci Biotechnol Biochem,
71,
38-46.
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D.Teng,
J.H.Wang,
Y.Fan,
Y.L.Yang,
Z.G.Tian,
J.Luo,
G.P.Yang,
and
F.Zhang
(2006).
Cloning of beta-1,3-1,4-glucanase gene from Bacillus licheniformis EGW039 (CGMCC 0635) and its expression in Escherichia coli BL21 (DE3).
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Appl Microbiol Biotechnol,
72,
705-712.
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E.Kitamura,
and
Y.Kamei
(2006).
Molecular cloning of the gene encoding beta-1,3(4)-glucanase A from a marine bacterium, Pseudomonas sp. PE2, an essential enzyme for the degradation of Pythium porphyrae cell walls.
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Appl Microbiol Biotechnol,
71,
630-637.
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G.Michel,
P.Nyval-Collen,
T.Barbeyron,
M.Czjzek,
and
W.Helbert
(2006).
Bioconversion of red seaweed galactans: a focus on bacterial agarases and carrageenases.
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Appl Microbiol Biotechnol,
71,
23-33.
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R.Kawai,
K.Igarashi,
M.Yoshida,
M.Kitaoka,
and
M.Samejima
(2006).
Hydrolysis of beta-1,3/1,6-glucan by glycoside hydrolase family 16 endo-1,3(4)-beta-glucanase from the basidiomycete Phanerochaete chrysosporium.
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Appl Microbiol Biotechnol,
71,
898-906.
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V.Receveur-Bréchot,
M.Czjzek,
A.Barre,
A.Roussel,
W.J.Peumans,
E.J.Van Damme,
and
P.Rougé
(2006).
Crystal structure at 1.45-A resolution of the major allergen endo-beta-1,3-glucanase of banana as a molecular basis for the latex-fruit syndrome.
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Proteins,
63,
235-242.
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PDB code:
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J.D.Palumbo,
G.Y.Yuen,
C.C.Jochum,
K.Tatum,
and
D.Y.Kobayashi
(2005).
Mutagenesis of beta-1,3-Glucanase Genes in Lysobacter enzymogenes Strain C3 Results in Reduced Biological Control Activity Toward Bipolaris Leaf Spot of Tall Fescue and Pythium Damping-Off of Sugar Beet.
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Phytopathology,
95,
701-707.
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M.Akita,
K.Kayatama,
Y.Hatada,
S.Ito,
and
K.Horikoshi
(2005).
A novel beta-glucanase gene from Bacillus halodurans C-125.
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FEMS Microbiol Lett,
248,
9.
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Z.Pang,
Y.N.Kang,
M.Ban,
M.Oda,
R.Kobayashi,
M.Ohnishi,
and
B.Mikami
(2005).
Crystallization and preliminary crystallographic analysis of endo-1,3-beta-glucanase from Arthrobacter sp.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
61,
68-70.
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A.Grassick,
P.G.Murray,
R.Thompson,
C.M.Collins,
L.Byrnes,
G.Birrane,
T.M.Higgins,
and
M.G.Tuohy
(2004).
Three-dimensional structure of a thermostable native cellobiohydrolase, CBH IB, and molecular characterization of the cel7 gene from the filamentous fungus, Talaromyces emersonii.
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Eur J Biochem,
271,
4495-4506.
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PDB code:
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J.Allouch,
W.Helbert,
B.Henrissat,
and
M.Czjzek
(2004).
Parallel substrate binding sites in a beta-agarase suggest a novel mode of action on double-helical agarose.
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Structure,
12,
623-632.
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PDB code:
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P.I.Kim,
and
K.C.Chung
(2004).
Production of an antifungal protein for control of Colletotrichum lagenarium by Bacillus amyloliquefaciens MET0908.
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FEMS Microbiol Lett,
234,
177-183.
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J.D.Palumbo,
R.F.Sullivan,
and
D.Y.Kobayashi
(2003).
Molecular characterization and expression in Escherichia coli of three beta-1,3-glucanase genes from Lysobacter enzymogenes strain N4-7.
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J Bacteriol,
185,
4362-4370.
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J.Walter,
N.C.Heng,
W.P.Hammes,
D.M.Loach,
G.W.Tannock,
and
C.Hertel
(2003).
Identification of Lactobacillus reuteri genes specifically induced in the mouse gastrointestinal tract.
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Appl Environ Microbiol,
69,
2044-2051.
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P.Johansson,
S.Denman,
H.Brumer,
A.M.Kallas,
H.Henriksson,
T.Bergfors,
T.T.Teeri,
and
T.A.Jones
(2003).
Crystallization and preliminary X-ray analysis of a xyloglucan endotransglycosylase from Populus tremula x tremuloides.
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Acta Crystallogr D Biol Crystallogr,
59,
535-537.
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G.Michel,
L.Chantalat,
E.Duee,
T.Barbeyron,
B.Henrissat,
B.Kloareg,
and
O.Dideberg
(2001).
The kappa-carrageenase of P. carrageenovora features a tunnel-shaped active site: a novel insight in the evolution of Clan-B glycoside hydrolases.
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Structure,
9,
513-525.
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PDB code:
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L.C.Tsai,
L.F.Shyur,
S.S.Lin,
and
H.S.Yuan
(2001).
Crystallization and preliminary X-ray diffraction analysis of the 1,3-1,4-beta-D-glucanase from Fibrobacter succinogenes.
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Acta Crystallogr D Biol Crystallogr,
57,
1303-1306.
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A.Planas
(2000).
Bacterial 1,3-1,4-beta-glucanases: structure, function and protein engineering.
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Biochim Biophys Acta,
1543,
361-382.
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B.O.Petersen,
M.Krah,
J.O.Duus,
and
K.K.Thomsen
(2000).
A transglycosylating 1,3(4)-beta-glucanase from rhodothermus marinus NMR analysis of enzyme reactions.
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Eur J Biochem,
267,
361-369.
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K.Piotukh,
V.Serra,
R.Borriss,
and
A.Planas
(1999).
Protein-carbohydrate interactions defining substrate specificity in Bacillus 1,3-1,4-beta-D-glucan 4-glucanohydrolases as dissected by mutational analysis.
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Biochemistry,
38,
16092-16104.
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J.Aÿ,
F.Götz,
R.Borriss,
and
U.Heinemann
(1998).
Structure and function of the Bacillus hybrid enzyme GluXyn-1: native-like jellyroll fold preserved after insertion of autonomous globular domain.
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Proc Natl Acad Sci U S A,
95,
6613-6618.
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PDB code:
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J.Aÿ,
M.Hahn,
K.Decanniere,
K.Piotukh,
R.Borriss,
and
U.Heinemann
(1998).
Crystal structures and properties of de novo circularly permuted 1,3-1,4-beta-glucanases.
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Proteins,
30,
155-167.
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PDB codes:
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J.L.Viladot,
E.de Ramon,
O.Durany,
and
A.Planas
(1998).
Probing the mechanism of Bacillus 1,3-1,4-beta-D-glucan 4-glucanohydrolases by chemical rescue of inactive mutants at catalytically essential residues.
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Biochemistry,
37,
11332-11342.
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P.E.Johnson,
A.L.Creagh,
E.Brun,
K.Joe,
P.Tomme,
C.A.Haynes,
and
L.P.McIntosh
(1998).
Calcium binding by the N-terminal cellulose-binding domain from Cellulomonas fimi beta-1,4-glucanase CenC.
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Biochemistry,
37,
12772-12781.
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B.Henrissat,
and
G.Davies
(1997).
Structural and sequence-based classification of glycoside hydrolases.
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Curr Opin Struct Biol,
7,
637-644.
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L.F.Mackenzie,
G.J.Davies,
M.Schülein,
and
S.G.Withers
(1997).
Identification of the catalytic nucleophile of endoglucanase I from Fusarium oxysporum by mass spectrometry.
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Biochemistry,
36,
5893-5901.
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N.C.Heng,
H.F.Jenkinson,
and
G.W.Tannock
(1997).
Cloning and expression of an endo-1,3-1,4-beta-glucanase gene from Bacillus macerans in Lactobacillus reuteri.
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Appl Environ Microbiol,
63,
3336-3340.
|
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K.Welfle,
R.Misselwitz,
O.Politz,
R.Borriss,
and
H.Welfle
(1996).
Individual amino acids in the N-terminal loop region determine the thermostability and unfolding characteristics of bacterial glucanases.
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Protein Sci,
5,
2255-2265.
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L.G.Jensen,
O.Olsen,
O.Kops,
N.Wolf,
K.K.Thomsen,
and
D.von Wettstein
(1996).
Transgenic barley expressing a protein-engineered, thermostable (1,3-1,4)-beta-glucanase during germination.
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Proc Natl Acad Sci U S A,
93,
3487-3491.
|
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P.E.Johnson,
M.D.Joshi,
P.Tomme,
D.G.Kilburn,
and
L.P.McIntosh
(1996).
Structure of the N-terminal cellulose-binding domain of Cellulomonas fimi CenC determined by nuclear magnetic resonance spectroscopy.
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Biochemistry,
35,
14381-14394.
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PDB codes:
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R.A.Warren
(1996).
Microbial hydrolysis of polysaccharides.
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Annu Rev Microbiol,
50,
183-212.
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D.D.Leonidas,
B.L.Elbert,
Z.Zhou,
H.Leffler,
S.J.Ackerman,
and
K.R.Acharya
(1995).
Crystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins.
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Structure,
3,
1379-1393.
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PDB code:
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M.Hahn,
T.Keitel,
and
U.Heinemann
(1995).
Crystal and molecular structure at 0.16-nm resolution of the hybrid Bacillus endo-1,3-1,4-beta-D-glucan 4-glucanohydrolase H(A16-M).
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Eur J Biochem,
232,
849-858.
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PDB code:
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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.
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}
}
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