2c71: Difference between revisions
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==About this Structure== | ==About this Structure== | ||
2C71 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 MG as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ | 2C71 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 MG as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Acetylxylan_esterase Acetylxylan esterase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.72 3.1.1.72]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C71 OCA]]. | ||
==Reference== | ==Reference== | ||
Structure and activity of two metal ion-dependent acetylxylan esterases involved in plant cell wall degradation reveals a close similarity to peptidoglycan deacetylases., Taylor EJ, Gloster TM, Turkenburg JP, Vincent F, Brzozowski AM, Dupont C, Shareck F, Centeno MS, Prates JA, Puchart V, Ferreira LM, Fontes CM, Biely P, Davies GJ, J Biol Chem. 2006 Apr 21;281(16):10968-75. Epub 2006 Jan 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16431911 16431911] | Structure and activity of two metal ion-dependent acetylxylan esterases involved in plant cell wall degradation reveals a close similarity to peptidoglycan deacetylases., Taylor EJ, Gloster TM, Turkenburg JP, Vincent F, Brzozowski AM, Dupont C, Shareck F, Centeno MS, Prates JA, Puchart V, Ferreira LM, Fontes CM, Biely P, Davies GJ, J Biol Chem. 2006 Apr 21;281(16):10968-75. Epub 2006 Jan 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16431911 16431911] | ||
[[Category: Acetylxylan esterase]] | |||
[[Category: Clostridium thermocellum]] | [[Category: Clostridium thermocellum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: metal-ion]] | [[Category: metal-ion]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:43:44 2007'' | ||
Revision as of 11:39, 30 October 2007
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THE STRUCTURE OF A FAMILY 4 ACETYL XYLAN ESTERASE FROM CLOSTRIDIUM THERMOCELLUM IN COMPLEX WITH A MAGNESIUM ION.
OverviewOverview
The enzymatic degradation of plant cell wall xylan requires the concerted, action of a diverse enzymatic syndicate. Among these enzymes are xylan, esterases, which hydrolyze the O-acetyl substituents, primarily at the O-2, position of the xylan backbone. All acetylxylan esterase structures, described previously display a alpha/beta hydrolase fold with a, "Ser-His-Asp" catalytic triad. Here we report the structures of two, distinct acetylxylan esterases, those from Streptomyces lividans and, Clostridium thermocellum, in native and complex forms, with x-ray data to, between 1.6 and 1.0 A resolution. We show, using a novel linked assay, system with PNP-2-O-acetylxyloside and a beta-xylosidase, that the enzymes, are sugar-specific and metal ion-dependent and possess a single metal, center ... [(full description)]
About this StructureAbout this Structure
2C71 is a [Single protein] structure of sequence from [Clostridium thermocellum] with MG as [ligand]. Active as [Acetylxylan esterase], with EC number [3.1.1.72]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Structure and activity of two metal ion-dependent acetylxylan esterases involved in plant cell wall degradation reveals a close similarity to peptidoglycan deacetylases., Taylor EJ, Gloster TM, Turkenburg JP, Vincent F, Brzozowski AM, Dupont C, Shareck F, Centeno MS, Prates JA, Puchart V, Ferreira LM, Fontes CM, Biely P, Davies GJ, J Biol Chem. 2006 Apr 21;281(16):10968-75. Epub 2006 Jan 23. PMID:16431911
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