1e5c
From Proteopedia
(New page: 200px<br /> <applet load="1e5c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e5c" /> '''INTERNAL XYLAN BINDING DOMAIN FROM C. FIMI ...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1E5C is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Cellulomonas_fimi Cellulomonas fimi]]. 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=1E5C OCA]]. | + | 1E5C is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Cellulomonas_fimi Cellulomonas fimi]]. 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: XBD. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E5C OCA]]. |
==Reference== | ==Reference== | ||
The structural basis for the ligand specificity of family 2 carbohydrate-binding modules., Simpson PJ, Xie H, Bolam DN, Gilbert HJ, Williamson MP, J Biol Chem. 2000 Dec 29;275(52):41137-42. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10973978 10973978] | The structural basis for the ligand specificity of family 2 carbohydrate-binding modules., Simpson PJ, Xie H, Bolam DN, Gilbert HJ, Williamson MP, J Biol Chem. 2000 Dec 29;275(52):41137-42. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10973978 10973978] | ||
[[Category: Cellulomonas fimi]] | [[Category: Cellulomonas fimi]] | ||
| + | [[Category: Endo-1,4-beta-xylanase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bolam, D.N.]] | [[Category: Bolam, D.N.]] | ||
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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 Tue Oct 30 10:51:52 2007'' |
Revision as of 08:47, 30 October 2007
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INTERNAL XYLAN BINDING DOMAIN FROM C. FIMI XYN10A, R262G MUTANT
Overview
The interactions of proteins with polysaccharides play a key role in the, microbial hydrolysis of cellulose and xylan, the most abundant organic, molecules in the biosphere, and are thus pivotal to the recycling of, photosynthetically fixed carbon. Enzymes that attack these recalcitrant, polymers have a modular structure comprising catalytic modules and, non-catalytic carbohydrate-binding modules (CBMs). The largest prokaryotic, CBM family, CBM2, contains members that bind cellulose (CBM2a) and xylan, (CBM2b), respectively. A possible explanation for the different ligand, specificity of CBM2b is that one of the surface tryptophans involved in, the protein-carbohydrate interaction is rotated by 90 degrees compared, with its position in CBM2a (thus matching the structure of the binding, ... [(full description)]
About this Structure
1E5C is a [Single protein] structure of sequence from [Cellulomonas fimi]. Active as [Endo-1,4-beta-xylanase], with EC number [3.2.1.8]. Structure known Active Site: XBD. Full crystallographic information is available from [OCA].
Reference
The structural basis for the ligand specificity of family 2 carbohydrate-binding modules., Simpson PJ, Xie H, Bolam DN, Gilbert HJ, Williamson MP, J Biol Chem. 2000 Dec 29;275(52):41137-42. PMID:10973978
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