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Article: Crystal structure of a heat-resilient phytase from Aspergillus fumigatus, carrying a phosphorylated histidine

TitleCrystal structure of a heat-resilient phytase from Aspergillus fumigatus, carrying a phosphorylated histidine
Authors
KeywordsA. fumigatus phytase
covalent reaction intermediate
crystal structure
heat-resistant
protein engineering
R.M.S., root-mean-square
Issue Date2004
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/jmb
Citation
Journal Of Molecular Biology, 2004, v. 339 n. 2, p. 437-445 How to Cite?
AbstractIn order to understand the structural basis for the high thermostability of phytase from Aspergillus fumigatus, its crystal structure was determined at 1.5Å resolution. The overall fold resembles the structure of other phytase enzymes. Aspergillus niger phytase shares 66% sequence identity, however, it is much less heat-resistant. A superimposition of these two structures reveals some significant differences. In particular, substitutions with polar residues appear to remove repulsive ion pair interactions and instead form hydrogen bond interactions, which stabilize the enzyme; the formation of a C-terminal helical capping, induced by arginine residue substitutions also appears to be critical for the enzyme's ability to refold to its active form after denaturation at high temperature. The heat-resilient property of A.fumigatus phytase could be due to the improved stability of regions that are critical for the refolding of the protein; and a heat-resistant A.niger phytase may be achieved by mutating certain critical residues with the equivalent residues in A.fumigatus phytase. Six predicted N-glycosylation sites were observed to be glycosylated from the experimental electron density. Furthermore, the enzyme's catalytic residue His59 was found to be partly phosphorylated and thus showed a reaction intermediate, providing structural insight, which may help understand the catalytic mechanism of the acid phosphatase family. The trap of this catalytic intermediate confirms the two-step catalytic mechanism of the acid histidine phosphatase family. © 2004 Elsevier Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/91927
ISSN
2015 Impact Factor: 4.517
2015 SCImago Journal Rankings: 3.002
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorXiang, Ten_HK
dc.contributor.authorLiu, Qen_HK
dc.contributor.authorDeacon, AMen_HK
dc.contributor.authorKoshy, Men_HK
dc.contributor.authorKriksunov, IAen_HK
dc.contributor.authorLei, XGen_HK
dc.contributor.authorHao, Qen_HK
dc.contributor.authorThiel, DJen_HK
dc.date.accessioned2010-09-17T10:30:46Z-
dc.date.available2010-09-17T10:30:46Z-
dc.date.issued2004en_HK
dc.identifier.citationJournal Of Molecular Biology, 2004, v. 339 n. 2, p. 437-445en_HK
dc.identifier.issn0022-2836en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91927-
dc.description.abstractIn order to understand the structural basis for the high thermostability of phytase from Aspergillus fumigatus, its crystal structure was determined at 1.5Å resolution. The overall fold resembles the structure of other phytase enzymes. Aspergillus niger phytase shares 66% sequence identity, however, it is much less heat-resistant. A superimposition of these two structures reveals some significant differences. In particular, substitutions with polar residues appear to remove repulsive ion pair interactions and instead form hydrogen bond interactions, which stabilize the enzyme; the formation of a C-terminal helical capping, induced by arginine residue substitutions also appears to be critical for the enzyme's ability to refold to its active form after denaturation at high temperature. The heat-resilient property of A.fumigatus phytase could be due to the improved stability of regions that are critical for the refolding of the protein; and a heat-resistant A.niger phytase may be achieved by mutating certain critical residues with the equivalent residues in A.fumigatus phytase. Six predicted N-glycosylation sites were observed to be glycosylated from the experimental electron density. Furthermore, the enzyme's catalytic residue His59 was found to be partly phosphorylated and thus showed a reaction intermediate, providing structural insight, which may help understand the catalytic mechanism of the acid phosphatase family. The trap of this catalytic intermediate confirms the two-step catalytic mechanism of the acid histidine phosphatase family. © 2004 Elsevier Ltd. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/jmben_HK
dc.relation.ispartofJournal of Molecular Biologyen_HK
dc.subjectA. fumigatus phytaseen_HK
dc.subjectcovalent reaction intermediateen_HK
dc.subjectcrystal structureen_HK
dc.subjectheat-resistanten_HK
dc.subjectprotein engineeringen_HK
dc.subjectR.M.S., root-mean-squareen_HK
dc.titleCrystal structure of a heat-resilient phytase from Aspergillus fumigatus, carrying a phosphorylated histidineen_HK
dc.typeArticleen_HK
dc.identifier.emailHao, Q: qhao@hku.hken_HK
dc.identifier.authorityHao, Q=rp01332en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.jmb.2004.03.057en_HK
dc.identifier.pmid15136045-
dc.identifier.scopuseid_2-s2.0-2342501800en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-2342501800&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume339en_HK
dc.identifier.issue2en_HK
dc.identifier.spage437en_HK
dc.identifier.epage445en_HK
dc.identifier.isiWOS:000221561800016-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridXiang, T=36958701000en_HK
dc.identifier.scopusauthoridLiu, Q=35215401600en_HK
dc.identifier.scopusauthoridDeacon, AM=7004891624en_HK
dc.identifier.scopusauthoridKoshy, M=7005340569en_HK
dc.identifier.scopusauthoridKriksunov, IA=6507909504en_HK
dc.identifier.scopusauthoridLei, XG=7202627277en_HK
dc.identifier.scopusauthoridHao, Q=7102508868en_HK
dc.identifier.scopusauthoridThiel, DJ=7005794841en_HK

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