1h1a
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1h1a |SIZE=350|CAPTION= <scene name='initialview01'>1h1a</scene>, resolution 1.75Å | |PDB= 1h1a |SIZE=350|CAPTION= <scene name='initialview01'>1h1a</scene>, resolution 1.75Å | ||
|SITE= <scene name='pdbsite=S1A:Gol+Binding+Site+For+Chain+A'>S1A</scene> | |SITE= <scene name='pdbsite=S1A:Gol+Binding+Site+For+Chain+A'>S1A</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=S:SULFUR+ATOM'>S</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h1a OCA], [http://www.ebi.ac.uk/pdbsum/1h1a PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h1a RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Hakulinen, N.]] | [[Category: Hakulinen, N.]] | ||
[[Category: Rouvinen, J.]] | [[Category: Rouvinen, J.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: S]] | ||
| - | [[Category: SO4]] | ||
[[Category: family 11]] | [[Category: family 11]] | ||
[[Category: glycosyl hydrolase]] | [[Category: glycosyl hydrolase]] | ||
| Line 34: | Line 33: | ||
[[Category: xylanase]] | [[Category: xylanase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:55:38 2008'' |
Revision as of 17:55, 30 March 2008
| |||||||
| , resolution 1.75Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , , | ||||||
| Activity: | Endo-1,4-beta-xylanase, with EC number 3.2.1.8 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Sun Mar 30 20:55:38 2008
