2c79
From Proteopedia
(New page: 200px<br /> <applet load="2c79" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c79, resolution 1.50Å" /> '''THE STRUCTURE OF A ...) |
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==About this Structure== | ==About this Structure== | ||
| - | 2C79 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 CO as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.72 3.1.1.72]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C79 OCA]]. | + | 2C79 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 CO as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Hydrolase Hydrolase]], 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=2C79 OCA]]. |
==Reference== | ==Reference== | ||
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[[Category: metal-ion]] | [[Category: metal-ion]] | ||
| - | ''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 08:44:06 2007'' |
Revision as of 06:39, 30 October 2007
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THE STRUCTURE OF A FAMILY 4 ACETYL XYLAN ESTERASE FROM CLOSTRIDIUM THERMOCELLUM IN COMPLEX WITH A COLBALT ION.
Overview
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 Structure
2C79 is a [Single protein] structure of sequence from [Clostridium thermocellum] with CO as [ligand]. Active as [Hydrolase], with EC number [3.1.1.72]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
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:16431911
Page seeded by OCA on Tue Oct 30 08:44:06 2007
Categories: Clostridium thermocellum | Single protein | Biely, P. | Brzozowski, A.M. | Centeno, M.S.J. | Davies, G.J. | Dupont, C. | Ferreira, L.M.A. | Fontes, C.M.G.A. | Gloster, T.M. | Prates, J.A.M. | Shareck, F. | Taylor, E.J. | Turkenburg, P.J. | Vincent, F. | CO | Acetyl-xylan | Esterases | Hydrolase | Metal-ion
