Multiple conformations of catalytic serine and histidine in acetylxylan esterase at 0.90 Å

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dc.contributor.authorGhosh, D
dc.contributor.authorSawicki, M
dc.contributor.authorLala, P
dc.contributor.authorErman, M
dc.contributor.authorPangborn, W
dc.contributor.authorEyzaguirre, J
dc.contributor.authorGutiérrez, R
dc.contributor.authorJörnvall, H
dc.contributor.authorThiel, DJ
dc.date.accessioned2025-01-21T01:30:54Z
dc.date.available2025-01-21T01:30:54Z
dc.date.issued2001
dc.description.abstractAcetylxylan esterase (AXEII; 207 amino acids) from Penicillium purpurogenum has substrate specificities toward acetate esters of D-xylopyranose residues in xylan and belongs to a new class of alpha/beta hydrolases. The crystal structure of AXEII has been determined by single isomorphous replacement and anomalous scattering, and refined at 0.90- and 1.10-Angstrom resolutions with data collected at 85 K and 295 K, respectively. The tertiary structure consists of a doubly wound alpha/beta sandwich, having a central six-stranded parallel beta -sheet flanked by two parallel ol-helices on each side. The catalytic residues Ser(90), His(187), and Ap(175) are located at the C-terminal end of the sheet, an exposed region of the molecule. The serine and histidine side chains in the 295 K structure show the frequently observed conformations in which Ser(90) is trans and the hydroxyl group is in the plane of the imidazole ring of His(187), However, the structure at 85 K displays an additional conformation in which Ser(90) side-chain hydroxyl is away from the plane of the imidazole ring of His(187). The His(187) side chain forms a hydrogen bond with a sulfate ion and adopts an altered conformation. The only other known hydrolase that has a similar tertiary structure is Fusarium solani cutinase, The exposed nature of the catalytic triad suggests that AXEII is a pure esterase, i.e. an alpha/beta hydrolase with specificity for nonlipidic polar substrates.
dc.fuente.origenWOS
dc.identifier.issn0021-9258
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/96924
dc.identifier.wosidWOS:000167980900078
dc.issue.numero14
dc.language.isoen
dc.pagina.final11166
dc.pagina.inicio11159
dc.revistaJournal of biological chemistry
dc.rightsacceso restringido
dc.subject.ods12 Responsible Consumption and Production
dc.subject.ods07 Affordable and Clean Energy
dc.subject.odspa12 Producción y consumo responsable
dc.subject.odspa07 Energía asequible y no contaminante
dc.titleMultiple conformations of catalytic serine and histidine in acetylxylan esterase at 0.90 Å
dc.typeartículo
dc.volumen276
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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