1od8
Xylanase Xyn10A from Streptomyces lividans in complex with xylobio-isofagomine lactamXylanase Xyn10A from Streptomyces lividans in complex with xylobio-isofagomine lactam
Structural highlights
FunctionXYNA_STRLI Contributes to hydrolyze hemicellulose, the major component of plant cell-walls. XLNA and XLNB seem to act sequentially on the substrate to yield xylobiose and xylose as carbon sources. Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe atomic-resolution structure of a xylobiose-derived isofagomine lactam in complex with the xylanase Xyn10A from Streptomyces lividans reveals that the lactam is bound to the enzyme as the amide tautomer, with "reversed" protonation-states for nucleophile and acid-base. A xylobiose-derived isofagomine lactam glycosidase inhibitor binds as its amide tautomer.,Gloster T, Williams SJ, Tarling CA, Roberts S, Dupont C, Jodoin P, Shareck F, Withers SG, Davies GJ Chem Commun (Camb). 2003 Apr 21;(8):944-5. PMID:12744311[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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