2c79: Difference between revisions
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[[Image:2c79.gif|left|200px]]<br /><applet load="2c79" size=" | [[Image:2c79.gif|left|200px]]<br /><applet load="2c79" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2c79, resolution 1.50Å" /> | caption="2c79, resolution 1.50Å" /> | ||
'''THE STRUCTURE OF A FAMILY 4 ACETYL XYLAN ESTERASE FROM CLOSTRIDIUM THERMOCELLUM IN COMPLEX WITH A COLBALT ION.'''<br /> | '''THE STRUCTURE OF A FAMILY 4 ACETYL XYLAN ESTERASE FROM CLOSTRIDIUM THERMOCELLUM IN COMPLEX WITH A COLBALT ION.'''<br /> | ||
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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/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] Known structural/functional Site: <scene name='pdbsite=AC1:Co Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http:// | 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 <scene name='pdbligand=CO:'>CO</scene> 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] Known structural/functional Site: <scene name='pdbsite=AC1:Co+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C79 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: metal-ion]] | [[Category: metal-ion]] | ||
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Revision as of 11:32, 3 February 2008
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THE STRUCTURE OF A FAMILY 4 ACETYL XYLAN ESTERASE FROM CLOSTRIDIUM THERMOCELLUM IN COMPLEX WITH A COLBALT 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 with a chemical preference for Co2+. Asp and His side chains, complete the catalytic machinery. Different metal ion preferences for the, two enzymes may reflect the surprising diversity with which the metal ion, coordinates residues and ligands in the active center environment of the, S. lividans and C. thermocellum enzymes. These "CE4" esterases involved in, plant cell wall degradation are shown to be closely related to the, de-N-acetylases involved in chitin and peptidoglycan degradation (Blair, D. E., Schuettelkopf, A. W., MacRae, J. I., and Aalten, D. M. (2005) Proc., Natl. Acad. Sci. U. S. A., 102, 15429-15434), which form the NodB, deacetylase "superfamily."
About this StructureAbout this Structure
2C79 is a Single protein structure of sequence from Clostridium thermocellum with as ligand. Active as Acetylxylan esterase, with EC number 3.1.1.72 Known structural/functional Site: . 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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