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PDBsum entry 1hix

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Hydrolase PDB id
1hix
Contents
Protein chains
185 a.a. *
Waters ×219
* Residue conservation analysis

References listed in PDB file
Key reference
Title Crystallographic analysis of family 11 endo-Beta-1,4-Xylanase xyl1 from streptomyces sp. S38.
Authors J.Wouters, J.Georis, D.Engher, J.Vandenhaute, J.Dusart, J.M.Frere, E.Depiereux, P.Charlier.
Ref. Acta Crystallogr D Biol Crystallogr, 2001, 57, 1813-1819. [DOI no: 10.1107/S0907444901015153]
PubMed id 11717493
Abstract
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.
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).
Figure 5.
Figure 5 Stereoview of the active site of Xyl1 from Streptomyces sp. S38.
The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2001, 57, 1813-1819) copyright 2001.
Secondary reference #1
Title An additional aromatic interaction improves the thermostability and thermophilicity of a mesophilic family 11 xylanase: structural basis and molecular study.
Authors J.Georis, F.De lemos esteves, J.Lamotte-Brasseur, V.Bougnet, B.Devreese, F.Giannotta, B.Granier, J.M.Frère.
Ref. Protein Sci, 2000, 9, 466-475. [DOI no: 10.1110/ps.9.3.466]
PubMed id 10752608
Full text Abstract
Secondary reference #2
Title Sequence, Overproduction and purification of the family 11 endo-Beta-1,4-Xylanase encoded by the xyl1 gene of streptomyces sp. S38.
Authors J.Georis, F.Giannotta, J.Lamotte-Brasseur, B.Devreese, J.Van beeumen, B.Granier, J.M.Frère.
Ref. Gene, 1999, 237, 123-133. [DOI no: 10.1016/S0378-1119(99)00311-X]
PubMed id 10524243
Full text Abstract
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