1h1a
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The crystal structures of thermophilic xylanases from Chaetomium, thermophilum and Nonomuraea flexuosa were determined at 1.75 and 2.1 A, resolution, respectively. Both enzymes have the overall fold typical to, family 11 xylanases with two highly twisted beta-sheets forming a large, cleft. The comparison of 12 crystal structures of family 11 xylanases from, both mesophilic and thermophilic organisms showed that the structures of, different xylanases are very similar. The sequence identity differences, correlated well with the structural differences. Several minor, modifications appeared to be responsible for the increased thermal, stability of family 11 xylanases: (a) higher Thr : Ser ratio (b) increased, number of charged residues, especially Arg, resulting in enhanced polar, .. | + | The crystal structures of thermophilic xylanases from Chaetomium, thermophilum and Nonomuraea flexuosa were determined at 1.75 and 2.1 A, resolution, respectively. Both enzymes have the overall fold typical to, family 11 xylanases with two highly twisted beta-sheets forming a large, cleft. The comparison of 12 crystal structures of family 11 xylanases from, both mesophilic and thermophilic organisms showed that the structures of, different xylanases are very similar. The sequence identity differences, correlated well with the structural differences. Several minor, modifications appeared to be responsible for the increased thermal, stability of family 11 xylanases: (a) higher Thr : Ser ratio (b) increased, number of charged residues, especially Arg, resulting in enhanced polar, interactions, and (c) improved stabilization of secondary structures, involved the higher number of residues in the beta-strands and, stabilization of the alpha-helix region. Some members of family 11, xylanases have a unique strategy to improve their stability, such as a, higher number of ion pairs or aromatic residues on protein surface, a more, compact structure, a tighter packing, and insertions at some regions, resulting in enhanced interactions. |
==About this Structure== | ==About this Structure== | ||
| - | 1H1A is a | + | 1H1A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chaetomium_thermophilum Chaetomium thermophilum] with SO4, CA, S and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] Structure known Active Site: S1A. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H1A OCA]. |
==Reference== | ==Reference== | ||
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[[Category: xylanase]] | [[Category: xylanase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:01:40 2007'' |
Revision as of 10:56, 5 November 2007
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THERMOPHILIC B-1,4-XYLANASE FROM CHAETOMIUM THERMOPHILUM
Overview
The crystal structures of thermophilic xylanases from Chaetomium, thermophilum and Nonomuraea flexuosa were determined at 1.75 and 2.1 A, resolution, respectively. Both enzymes have the overall fold typical to, family 11 xylanases with two highly twisted beta-sheets forming a large, cleft. The comparison of 12 crystal structures of family 11 xylanases from, both mesophilic and thermophilic organisms showed that the structures of, different xylanases are very similar. The sequence identity differences, correlated well with the structural differences. Several minor, modifications appeared to be responsible for the increased thermal, stability of family 11 xylanases: (a) higher Thr : Ser ratio (b) increased, number of charged residues, especially Arg, resulting in enhanced polar, interactions, and (c) improved stabilization of secondary structures, involved the higher number of residues in the beta-strands and, stabilization of the alpha-helix region. Some members of family 11, xylanases have a unique strategy to improve their stability, such as a, higher number of ion pairs or aromatic residues on protein surface, a more, compact structure, a tighter packing, and insertions at some regions, resulting in enhanced interactions.
About this Structure
1H1A is a Single protein structure of sequence from Chaetomium thermophilum with SO4, CA, S and GOL as ligands. Active as Endo-1,4-beta-xylanase, with EC number 3.2.1.8 Structure known Active Site: S1A. Full crystallographic information is available from OCA.
Reference
Three-dimensional structures of thermophilic beta-1,4-xylanases from Chaetomium thermophilum and Nonomuraea flexuosa. Comparison of twelve xylanases in relation to their thermal stability., Hakulinen N, Turunen O, Janis J, Leisola M, Rouvinen J, Eur J Biochem. 2003 Apr;270(7):1399-412. PMID:12653995
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