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PDBsum entry 1hix
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystallographic analysis of family 11 endo-Beta-1,4-Xylanase xyl1 from streptomyces sp. S38.
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Authors
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J.Wouters,
J.Georis,
D.Engher,
J.Vandenhaute,
J.Dusart,
J.M.Frere,
E.Depiereux,
P.Charlier.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2001,
57,
1813-1819.
[DOI no: ]
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PubMed id
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Abstract
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Family 11 endo-beta-1,4-xylanases degrade xylan, the main constituent of plant
hemicelluloses, and have many potential uses in biotechnology. The structure of
Xyl1, a family 11 endo-xylanase from Streptomyces sp. S38, has been solved. The
protein crystallized from ammonium sulfate in the trigonal space group P321,
with unit-cell parameters a = b = 71.49, c = 130.30 A, gamma = 120.0 degrees.
The structure was solved at 2.0 A by X-ray crystallography using the
molecular-replacement method and refined to a final R factor of 18.5% (R(free) =
26.9%). Xyl1 has the overall fold characteristic of family 11 xylanases, with
two highly twisted beta-sheets defining a long cleft containing the two
catalytic residues Glu87 and Glu177.
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Figure 4.
Figure 4 (a) Topologies of family 11 endo-xylanases allowing the
separation of those enzymes into two groups. Exs 11 type I:
endo-xylanases from T. reseei XYNI ([220]1xyn ), A. niger
([221]1ukr ), A. kawachii ([222]1bk1 ), B. circulans ([223]1bcx
). Exs 11 type II: endo-xylanases from T. reseei XYNII
([224]1xyp ), T. lanuginosa ([225]1yna ), T. harzianum
([226]1xnd ), P. varioti ([227]1pvx ), B. agaradhaerens
([228]1qh6 ), D. thermophilum XynB ([229]1f5j ). An enlargement
of the arrangement of the secondary elements around the
N-terminal region of Exs 11 is presented in (b).
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Figure 5.
Figure 5 Stereoview of the active site of Xyl1 from Streptomyces
sp. S38.
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2001,
57,
1813-1819)
copyright 2001.
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Secondary reference #1
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Title
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An additional aromatic interaction improves the thermostability and thermophilicity of a mesophilic family 11 xylanase: structural basis and molecular study.
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Authors
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J.Georis,
F.De lemos esteves,
J.Lamotte-Brasseur,
V.Bougnet,
B.Devreese,
F.Giannotta,
B.Granier,
J.M.Frère.
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Ref.
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Protein Sci, 2000,
9,
466-475.
[DOI no: ]
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PubMed id
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Secondary reference #2
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Title
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Sequence, Overproduction and purification of the family 11 endo-Beta-1,4-Xylanase encoded by the xyl1 gene of streptomyces sp. S38.
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Authors
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J.Georis,
F.Giannotta,
J.Lamotte-Brasseur,
B.Devreese,
J.Van beeumen,
B.Granier,
J.M.Frère.
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Ref.
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Gene, 1999,
237,
123-133.
[DOI no: ]
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PubMed id
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