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PDBsum entry 2cjl
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* Residue conservation analysis
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Enzyme class:
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E.C.3.2.1.14
- chitinase.
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Reaction:
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Hydrolysis of the 1,4-beta-linkages of N-acetyl-D-glucosamine polymers of chitin.
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Febs J
273:4889-4900
(2006)
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PubMed id:
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Crystal structure and enzymatic properties of a bacterial family 19 chitinase reveal differences from plant enzymes.
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I.A.Hoell,
B.Dalhus,
E.B.Heggset,
S.I.Aspmo,
V.G.Eijsink.
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ABSTRACT
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We describe the cloning, overexpression, purification, characterization and
crystal structure of chitinase G, a single-domain family 19 chitinase from the
Gram-positive bacterium Streptomyces coelicolor A3(2). Although chitinase G was
not capable of releasing 4-methylumbelliferyl from artificial
chitooligosaccharide substrates, it was capable of degrading longer
chitooligosaccharides at rates similar to those observed for other chitinases.
The enzyme was also capable of degrading a colored colloidal chitin substrate
(carboxymethyl-chitin-remazol-brilliant violet) and a small, presumably
amorphous, subfraction of alpha-chitin and beta-chitin, but was not capable of
degrading crystalline chitin completely. The crystal structures of chitinase G
and a related Streptomyces chitinase, chitinase C [Kezuka Y, Ohishi M, Itoh Y,
Watanabe J, Mitsutomi M, Watanabe T & Nonaka T (2006) J Mol Biol358,
472-484], showed that these bacterial family 19 chitinases lack several loops
that extend the substrate-binding grooves in family 19 chitinases from plants.
In accordance with these structural features, detailed analysis of the
degradation of chitooligosaccharides by chitinase G showed that the enzyme has
only four subsites (- 2 to + 2), as opposed to six (- 3 to + 3) for plant
enzymes. The most prominent structural difference leading to reduced size of the
substrate-binding groove is the deletion of a 13-residue loop between the two
putatively catalytic glutamates. The importance of these two residues for
catalysis was confirmed by a site-directed mutagenesis study.
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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.Taira,
Y.Mahoe,
N.Kawamoto,
S.Onaga,
H.Iwasaki,
T.Ohnuma,
and
T.Fukamizo
(2011).
Cloning and characterization of a small family 19 chitinase from moss (Bryum coronatum).
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Glycobiology,
21,
644-654.
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H.Li,
and
L.H.Greene
(2010).
Sequence and structural analysis of the chitinase insertion domain reveals two conserved motifs involved in chitin-binding.
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PLoS One,
5,
e8654.
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H.Tsuji,
S.Nishimura,
T.Inui,
Y.Kado,
K.Ishikawa,
T.Nakamura,
and
K.Uegaki
(2010).
Kinetic and crystallographic analyses of the catalytic domain of chitinase from Pyrococcus furiosus- the role of conserved residues in the active site.
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FEBS J,
277,
2683-2695.
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PDB codes:
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N.A.Udaya Prakash,
M.Jayanthi,
R.Sabarinathan,
P.Kangueane,
L.Mathew,
and
K.Sekar
(2010).
Evolution, homology conservation, and identification of unique sequence signatures in GH19 family chitinases.
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J Mol Evol,
70,
466-478.
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Y.Kezuka,
M.Kojima,
R.Mizuno,
K.Suzuki,
T.Watanabe,
and
T.Nonaka
(2010).
Structure of full-length class I chitinase from rice revealed by X-ray crystallography and small-angle X-ray scattering.
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Proteins,
78,
2295-2305.
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PDB code:
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M.E.Lacombe-Harvey,
T.Fukamizo,
J.Gagnon,
M.G.Ghinet,
N.Dennhart,
T.Letzel,
and
R.Brzezinski
(2009).
Accessory active site residues of Streptomyces sp. N174 chitosanase: variations on a common theme in the lysozyme superfamily.
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FEBS J,
276,
857-869.
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W.Ubhayasekera,
R.Rawat,
S.W.Ho,
M.Wiweger,
S.Von Arnold,
M.L.Chye,
and
S.L.Mowbray
(2009).
The first crystal structures of a family 19 class IV chitinase: the enzyme from Norway spruce.
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Plant Mol Biol,
71,
277-289.
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PDB codes:
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J.Huet,
M.Azarkan,
Y.Looze,
V.Villeret,
and
R.Wintjens
(2008).
Crystallization and preliminary X-ray analysis of a family 19 glycosyl hydrolase from Carica papaya latex.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
64,
371-374.
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Y.Honda,
H.Taniguchi,
and
M.Kitaoka
(2008).
A reducing-end-acting chitinase from Vibrio proteolyticus belonging to glycoside hydrolase family 19.
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Appl Microbiol Biotechnol,
78,
627-634.
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W.Ubhayasekera,
C.M.Tang,
S.W.Ho,
G.Berglund,
T.Bergfors,
M.L.Chye,
and
S.L.Mowbray
(2007).
Crystal structures of a family 19 chitinase from Brassica juncea show flexibility of binding cleft loops.
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FEBS J,
274,
3695-3703.
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PDB codes:
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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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Links
