1m4w

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[[Image:1m4w.jpg|left|200px]]
[[Image:1m4w.jpg|left|200px]]
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{{Structure
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|PDB= 1m4w |SIZE=350|CAPTION= <scene name='initialview01'>1m4w</scene>, resolution 2.1&Aring;
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The line below this paragraph, containing "STRUCTURE_1m4w", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1m4w| PDB=1m4w | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m4w OCA], [http://www.ebi.ac.uk/pdbsum/1m4w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m4w RCSB]</span>
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'''Thermophilic b-1,4-xylanase from Nonomuraea flexuosa'''
'''Thermophilic b-1,4-xylanase from Nonomuraea flexuosa'''
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[[Category: Rouvinen, J.]]
[[Category: Rouvinen, J.]]
[[Category: Turunen, O]]
[[Category: Turunen, O]]
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[[Category: family 11]]
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[[Category: Family 11]]
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[[Category: glycosyl hydrolase]]
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[[Category: Glycosyl hydrolase]]
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[[Category: thermostability]]
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[[Category: Thermostability]]
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[[Category: xylanase]]
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[[Category: Xylanase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:38:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:11:20 2008''
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Revision as of 21:38, 2 May 2008

Template:STRUCTURE 1m4w

Thermophilic b-1,4-xylanase from Nonomuraea flexuosa


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

1M4W is a Single protein structure of sequence from Thermopolyspora flexuosa. 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 Sat May 3 00:38:03 2008

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