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PDBsum entry 3w6c
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PDB id:
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Hydrolase
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Title:
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Crystal structure of catalytic domain of chitinase from ralstonia sp. A-471 in complex with disaccharide
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Structure:
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Lysozyme-like chitinolytic enzyme. Chain: a, b, c, d. Fragment: catalytic domain, unp residues 89-252. Engineered: yes
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Source:
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Ralstonia. Organism_taxid: 200912. Strain: a-471. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.00Å
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R-factor:
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0.182
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R-free:
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0.226
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Authors:
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T.Arimori,N.Kawamoto,N.Okazaki,M.Nakazawa,K.Miyatake,T.Fukamizo, M.Ueda,T.Tamada
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Key ref:
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T.Arimori
et al.
(2013).
Crystal structures of the catalytic domain of a novel glycohydrolase family 23 chitinase from Ralstonia sp. A-471 reveals a unique arrangement of the catalytic residues for inverting chitin hydrolysis.
J Biol Chem,
288,
18696-18706.
PubMed id:
DOI:
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Date:
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14-Feb-13
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Release date:
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15-May-13
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PROCHECK
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Headers
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References
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B7XCV4
(B7XCV4_9RALS) -
Lysozyme-like chitinolytic enzyme from Ralstonia sp. A-471
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Seq:
Struc:
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252 a.a.
151 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.3.2.1.14
- 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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DOI no:
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J Biol Chem
288:18696-18706
(2013)
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PubMed id:
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Crystal structures of the catalytic domain of a novel glycohydrolase family 23 chitinase from Ralstonia sp. A-471 reveals a unique arrangement of the catalytic residues for inverting chitin hydrolysis.
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T.Arimori,
N.Kawamoto,
S.Shinya,
N.Okazaki,
M.Nakazawa,
K.Miyatake,
T.Fukamizo,
M.Ueda,
T.Tamada.
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ABSTRACT
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Chitinase C from Ralstonia sp. A-471 (Ra-ChiC) has a catalytic domain sequence
similar to goose-type (G-type) lysozymes and, unlike other chitinases, belongs
to glycohydrolase (GH) family 23. Using NMR spectroscopy, however, Ra-ChiC was
found to interact only with the chitin dimer but not with the peptidoglycan
fragment. Here we report the crystal structures of wild-type, E141Q, and E162Q
of the catalytic domain of Ra-ChiC with or without chitin oligosaccharides.
Ra-ChiC has a substrate-binding site including a tunnel-shaped cavity, which
determines the substrate specificity. Mutation analyses based on this structural
information indicated that a highly conserved Glu-141 acts as a catalytic acid,
and that Asp-226 located at the roof of the tunnel activates a water molecule as
a catalytic base. The unique arrangement of the catalytic residues makes a clear
contrast to the other GH23 members and also to inverting GH19 chitinases.
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