1ukr
From Proteopedia
(New page: 200px<br /> <applet load="1ukr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ukr, resolution 2.4Å" /> '''STRUCTURE OF ENDO-1,...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1UKR is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UKR OCA]]. | + | 1UKR is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]]. 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 Sites: EA, EB, EC and ED. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UKR OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8890913 8890913] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8890913 8890913] | ||
[[Category: Aspergillus niger]] | [[Category: Aspergillus niger]] | ||
| + | [[Category: Endo-1,4-beta-xylanase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dijkstra, B.W.]] | [[Category: Dijkstra, B.W.]] | ||
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[[Category: xylan degradation]] | [[Category: xylan degradation]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:46:37 2007'' |
Revision as of 10:41, 30 October 2007
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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 ... [(full description)]
About this Structure
1UKR is a [Single protein] structure of sequence from [Aspergillus niger]. Active as [Endo-1,4-beta-xylanase], with EC number [3.2.1.8]. Structure known Active Sites: EA, EB, EC and ED. 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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