2c71: Difference between revisions
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|PDB= 2c71 |SIZE=350|CAPTION= <scene name='initialview01'>2c71</scene>, resolution 1.05Å | |PDB= 2c71 |SIZE=350|CAPTION= <scene name='initialview01'>2c71</scene>, resolution 1.05Å | ||
|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+A'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | ||
|ACTIVITY= [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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c71 OCA], [http://www.ebi.ac.uk/pdbsum/2c71 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2c71 RCSB]</span> | |||
}} | }} | ||
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[[Category: Turkenburg, P J.]] | [[Category: Turkenburg, P J.]] | ||
[[Category: Vincent, F.]] | [[Category: Vincent, F.]] | ||
[[Category: acetyl-xylan]] | [[Category: acetyl-xylan]] | ||
[[Category: esterase]] | [[Category: esterase]] | ||
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[[Category: metal-ion]] | [[Category: metal-ion]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:17:16 2008'' | ||
Revision as of 02:17, 31 March 2008
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| , resolution 1.05Å | |||||||
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| Activity: | Acetylxylan esterase, with EC number 3.1.1.72 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 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
2C71 is a Single protein structure of sequence from Clostridium thermocellum. 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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