1ukr
From Proteopedia
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|SITE= <scene name='pdbsite=EA:GLU+A+79+And+GLU+A+170+Refer+To+The+Catalytic+Acidic+Res+...'>EA</scene>, <scene name='pdbsite=EB:GLU+B+79+And+GLU+B+170+Refer+To+The+Catalytic+Acidic+Res+...'>EB</scene>, <scene name='pdbsite=EC:GLU+C+79+And+GLU+C+170+Refer+To+The+Catalytic+Acidic+Res+...'>EC</scene> and <scene name='pdbsite=ED:GLU+D+79+And+GLU+D+170+Refer+To+The+Catalytic+Acidic+Res+...'>ED</scene> | |SITE= <scene name='pdbsite=EA:GLU+A+79+And+GLU+A+170+Refer+To+The+Catalytic+Acidic+Res+...'>EA</scene>, <scene name='pdbsite=EB:GLU+B+79+And+GLU+B+170+Refer+To+The+Catalytic+Acidic+Res+...'>EB</scene>, <scene name='pdbsite=EC:GLU+C+79+And+GLU+C+170+Refer+To+The+Catalytic+Acidic+Res+...'>EC</scene> and <scene name='pdbsite=ED:GLU+D+79+And+GLU+D+170+Refer+To+The+Catalytic+Acidic+Res+...'>ED</scene> | ||
|LIGAND= | |LIGAND= | ||
| - | |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=1ukr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ukr OCA], [http://www.ebi.ac.uk/pdbsum/1ukr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ukr RCSB]</span> | ||
}} | }} | ||
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[[Category: xylan degradation]] | [[Category: xylan degradation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:11:35 2008'' |
Revision as of 21:11, 30 March 2008
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| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , and | ||||||
| Activity: | Endo-1,4-beta-xylanase, with EC number 3.2.1.8 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF ENDO-1,4-BETA-XYLANASE C
Overview
The crystal structure of endo-1,4-beta-xylanase I from Aspergillus niger has been solved by molecular replacement and was refined to 2.4 A resolution. The final R-factor for all data from 6 to 2.4 A is 17.9%. The A. niger xylanase has a characteristic fold which is unique for family G xylanases (root-mean-square deviation = 1.1 A to Trichoderma reesei xylanase I, which has 53% sequence identity). It consists of a single domain composed predominantly of beta-strands. Two beta-sheets are twisted around a deep, long cleft, which is lined with many aromatic amino acid residues and is large enough to accommodate at least four xylose residues. The two conserved glutamate residues, Glu79 and Glu170, which are likely to be involved in catalysis, reach into this cleft from opposite sides. A niger xylanase I is of particular commercial interest because of its low pH optimum. A model is proposed which explains this low pH optimum compared to other members of xylanase family G.
About this Structure
1UKR is a Single protein structure of sequence from Aspergillus niger. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of Endo-1,4-beta-xylanase I from Aspergillus niger: molecular basis for its low pH optimum., Krengel U, Dijkstra BW, J Mol Biol. 1996 Oct 18;263(1):70-8. PMID:8890913
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