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PDBsum entry 1knm
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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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Streptomyces lividans xylan binding domain cbm13 in complex with lactose
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Structure:
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Endo-1,4-beta-xylanase a. Chain: a. Fragment: carbohydrate binding module (residues 348-477). Synonym: xylanase a, 1,4-beta-d-xylan xylanohydrolase a. Engineered: yes
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Source:
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Streptomyces lividans. Organism_taxid: 1916. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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1.20Å
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R-factor:
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0.126
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R-free:
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0.169
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Authors:
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V.Notenboom,A.B.Boraston,S.J.Williams,D.G.Kilburn,D.R.Rose
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Key ref:
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V.Notenboom
et al.
(2002).
High-resolution crystal structures of the lectin-like xylan binding domain from Streptomyces lividans xylanase 10A with bound substrates reveal a novel mode of xylan binding.
Biochemistry,
41,
4246-4254.
PubMed id:
DOI:
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Date:
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19-Dec-01
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Release date:
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19-Jun-02
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PROCHECK
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Headers
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References
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P26514
(XYNA_STRLI) -
Endo-1,4-beta-xylanase A from Streptomyces lividans
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Seq: Struc:
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477 a.a.
129 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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Enzyme class:
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E.C.3.2.1.8
- endo-1,4-beta-xylanase.
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Reaction:
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Endohydrolysis of 1,4-beta-D-xylosidic linkages in xylans.
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DOI no:
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Biochemistry
41:4246-4254
(2002)
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PubMed id:
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High-resolution crystal structures of the lectin-like xylan binding domain from Streptomyces lividans xylanase 10A with bound substrates reveal a novel mode of xylan binding.
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V.Notenboom,
A.B.Boraston,
S.J.Williams,
D.G.Kilburn,
D.R.Rose.
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ABSTRACT
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Carbohydrate-binding module (CBM) family 13 includes the "R-type" or "ricin
superfamily" beta-trefoil lectins. The C-terminal CBM, CBM13, of xylanase 10A
from Streptomyces lividans is a family 13 CBM that is not only structurally
similar to the "R-type" lectins but also somewhat functionally similar. The
primary function of CBM13 is to bind the polysaccharide xylan, but it retains
the ability of the R-type lectins to bind small sugars such as lactose and
galactose. The association of CBM13 with xylan appears to involve cooperative
and additive participation of three binding pockets in each of the three trefoil
domains of CBM13, suggesting a novel mechanism of CBM-xylan interaction. Thus,
the interaction of CBM13 with sugars displays considerable plasticity for which
we provide a structural rationale. The high-resolution crystal structure of
CBM13 was determined by multiple anomalous dispersion from a complex of CBM13
with a brominated ligand. Crystal structures of CBM13 in complex with lactose
and xylopentaose revealed two distinct mechanisms of ligand binding. CBM13 has
retained its specificity for lactose via Ricin-like binding in all of the three
classic trefoil binding pockets. However, CBM13 has the ability to bind either
the nonreducing galactosyl moiety or the reducing glucosyl moiety of lactose.
The mode of xylopentaose binding suggests adaptive mutations in the trefoil
sugar binding scaffold to accommodate internal binding on helical polymers of
xylose.
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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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J.P.Yang,
X.X.Ma,
Y.X.He,
W.F.Li,
Y.Kang,
R.Bao,
Y.Chen,
and
C.Z.Zhou
(2011).
Crystal structure of the 30K protein from the silkworm Bombyx mori reveals a new member of the β-trefoil superfamily.
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J Struct Biol,
175,
97.
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PDB code:
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H.Hemmi,
A.Kuno,
S.Ito,
R.Suzuki,
T.Hasegawa,
and
J.Hirabayashi
(2009).
NMR studies on the interaction of sugars with the C-terminal domain of an R-type lectin from the earthworm Lumbricus terrestris.
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FEBS J,
276,
2095-2105.
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L.Maveyraud,
H.Niwa,
V.Guillet,
D.I.Svergun,
P.V.Konarev,
R.A.Palmer,
W.J.Peumans,
P.Rougé,
E.J.Van Damme,
C.D.Reynolds,
and
L.Mourey
(2009).
Structural basis for sugar recognition, including the Tn carcinoma antigen, by the lectin SNA-II from Sambucus nigra.
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Proteins,
75,
89.
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PDB codes:
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G.André-Leroux,
J.G.Berrin,
J.Georis,
F.Arnaut,
and
N.Juge
(2008).
Structure-based mutagenesis of Penicillium griseofulvum xylanase using computational design.
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Proteins,
72,
1298-1307.
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J.Kleine,
and
W.Liebl
(2006).
Comparative characterization of deletion derivatives of the modular xylanase XynA of Thermotoga maritima.
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Extremophiles,
10,
373-381.
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L.E.Taylor,
B.Henrissat,
P.M.Coutinho,
N.A.Ekborg,
S.W.Hutcheson,
and
R.M.Weiner
(2006).
Complete cellulase system in the marine bacterium Saccharophagus degradans strain 2-40T.
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J Bacteriol,
188,
3849-3861.
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J.Flint,
D.N.Bolam,
D.Nurizzo,
E.J.Taylor,
M.P.Williamson,
C.Walters,
G.J.Davies,
and
H.J.Gilbert
(2005).
Probing the mechanism of ligand recognition in family 29 carbohydrate-binding modules.
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J Biol Chem,
280,
23718-23726.
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PDB codes:
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V.Spiwok,
P.Lipovová,
T.Skálová,
E.Vondrácková,
J.Dohnálek,
J.Hasek,
and
B.Králová
(2005).
Modelling of carbohydrate-aromatic interactions: ab initio energetics and force field performance.
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J Comput Aided Mol Des,
19,
887-901.
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A.Miyanaga,
T.Koseki,
H.Matsuzawa,
T.Wakagi,
H.Shoun,
and
S.Fushinobu
(2004).
Crystal structure of a family 54 alpha-L-arabinofuranosidase reveals a novel carbohydrate-binding module that can bind arabinose.
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J Biol Chem,
279,
44907-44914.
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PDB codes:
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J.L.Henshaw,
D.N.Bolam,
V.M.Pires,
M.Czjzek,
B.Henrissat,
L.M.Ferreira,
C.M.Fontes,
and
H.J.Gilbert
(2004).
The family 6 carbohydrate binding module CmCBM6-2 contains two ligand-binding sites with distinct specificities.
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J Biol Chem,
279,
21552-21559.
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M.S.Sujatha,
and
P.V.Balaji
(2004).
Identification of common structural features of binding sites in galactose-specific proteins.
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Proteins,
55,
44-65.
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R.Suzuki,
Z.Fujimoto,
A.Kuno,
J.Hirabayashi,
K.Kasai,
and
T.Hasegawa
(2004).
Crystallization and preliminary X-ray crystallographic studies of the C-terminal domain of galactose-binding lectin EW29 from the earthworm Lumbricus terrestris.
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Acta Crystallogr D Biol Crystallogr,
60,
1895-1896.
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Y.Brennan,
W.N.Callen,
L.Christoffersen,
P.Dupree,
F.Goubet,
S.Healey,
M.Hernández,
M.Keller,
K.Li,
N.Palackal,
A.Sittenfeld,
G.Tamayo,
S.Wells,
G.P.Hazlewood,
E.J.Mathur,
J.M.Short,
D.E.Robertson,
and
B.A.Steer
(2004).
Unusual microbial xylanases from insect guts.
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Appl Environ Microbiol,
70,
3609-3617.
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Z.Fujimoto,
S.Kaneko,
A.Kuno,
H.Kobayashi,
I.Kusakabe,
and
H.Mizuno
(2004).
Crystal structures of decorated xylooligosaccharides bound to a family 10 xylanase from Streptomyces olivaceoviridis E-86.
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J Biol Chem,
279,
9606-9614.
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PDB codes:
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D.Shallom,
and
Y.Shoham
(2003).
Microbial hemicellulases.
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Curr Opin Microbiol,
6,
219-228.
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R.Olson,
and
E.Gouaux
(2003).
Vibrio cholerae cytolysin is composed of an alpha-hemolysin-like core.
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Protein Sci,
12,
379-383.
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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
code is
shown on the right.
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