1wb5: Difference between revisions
New page: left|200px<br /> <applet load="1wb5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wb5, resolution 1.40Å" /> '''S954A MUTANT OF THE... |
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==About this Structure== | ==About this Structure== | ||
1WB5 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum]] with ACT, CD, SYR and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. 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=1WB5 OCA]]. | 1WB5 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum]] with ACT, CD, SYR and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. 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: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WB5 OCA]]. | ||
==Reference== | ==Reference== | ||
Molecular determinants of substrate specificity in the feruloyl esterase module of xylanase 10B from Clostridium thermocellum., Tarbouriech N, Prates JA, Fontes CM, Davies GJ, Acta Crystallogr D Biol Crystallogr. 2005 Feb;61(Pt 2):194-7. Epub 2005, Jan 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15681871 15681871] | Molecular determinants of substrate specificity in the feruloyl esterase module of xylanase 10B from Clostridium thermocellum., Tarbouriech N, Prates JA, Fontes CM, Davies GJ, Acta Crystallogr D Biol Crystallogr. 2005 Feb;61(Pt 2):194-7. Epub 2005, Jan 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15681871 15681871] | ||
[[Category: Clostridium thermocellum]] | [[Category: Clostridium thermocellum]] | ||
[[Category: Endo-1,4-beta-xylanase]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Davies, G.J.]] | [[Category: Davies, G.J.]] | ||
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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 12:13:26 2007'' | ||
Revision as of 13:08, 30 October 2007
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S954A MUTANT OF THE FERULOYL ESTERASE MODULE FROM CLOSTRIDIUM THERMOCELLUM COMPLEXED WITH SYRINGATE
OverviewOverview
Feruloyl esterases play a key role in the degradation of the intricate, structure of the plant cell wall by hydrolysing the ferulate ester groups, involved in the cross-linking between hemicelluloses and between, hemicellulose and lignin. The structure of the feruloyl esterase module of, Clostridium thermocellum cellulosomal xylanase 10B has been reported, previously. It displays the alpha/beta hydrolase fold with a classical, Ser-His-Asp catalytic triad. Here, the structures of a Ser-Ala mutant of, this feruloyl esterase in complexes with methyl syringate, methyl, sinapinate and methyl vanillate are described. Substrate binding is, accompanied by subtle conformational changes at amino acids Trp982, Met955, Asn1023 and Ile1019 in the ligand-binding cavity. The structural, determinants, ... [(full description)]
About this StructureAbout this Structure
1WB5 is a [Single protein] structure of sequence from [Clostridium thermocellum] with ACT, CD, SYR and GOL as [ligands]. Active as [Endo-1,4-beta-xylanase], with EC number [3.2.1.8]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Molecular determinants of substrate specificity in the feruloyl esterase module of xylanase 10B from Clostridium thermocellum., Tarbouriech N, Prates JA, Fontes CM, Davies GJ, Acta Crystallogr D Biol Crystallogr. 2005 Feb;61(Pt 2):194-7. Epub 2005, Jan 19. PMID:15681871
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