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Article: The atomic resolution crystal structure of atratoxin determined by single wavelength anomalous diffraction phasing

TitleThe atomic resolution crystal structure of atratoxin determined by single wavelength anomalous diffraction phasing
Authors
Issue Date2004
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 2004, v. 279 n. 37, p. 39094-39104 How to Cite?
AbstractBy using single wavelength anomalous diffraction phasing based on the anomalous signal from copper atoms, the crystal structure of atratoxin was determined at the resolution of 1.5 Å and was refined to an ultrahigh resolution of 0.87 Å. The ultrahigh resolution electron density maps allowed the modeling of 38 amino acid residues in alternate conformations and the location of 322 of 870 possible hydrogen atoms. To get accurate information at the atomic level, atratosin-b (an analog of atratoxin with reduced toxicity) was also refined to an atomic resolution of 0.92 Å. By the sequence and structural comparison of these two atratoxins, Arg33 and Arg 36 were identified to be critical to their varied toxicity. The effect of copper ions on the distribution of hydrogen atoms in atratoxin was discussed, and the interactions between copper ions and protein residues were analyzed based on a statistical method, revealing a novel pentahedral copper-binding motif.
Persistent Identifierhttp://hdl.handle.net/10722/91901
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLou, Xen_HK
dc.contributor.authorLiu, Qen_HK
dc.contributor.authorTu, Xen_HK
dc.contributor.authorWang, Jen_HK
dc.contributor.authorTeng, Men_HK
dc.contributor.authorNiu, Len_HK
dc.contributor.authorSchuller, DJen_HK
dc.contributor.authorHuang, Qen_HK
dc.contributor.authorHao, Qen_HK
dc.date.accessioned2010-09-17T10:30:00Z-
dc.date.available2010-09-17T10:30:00Z-
dc.date.issued2004en_HK
dc.identifier.citationJournal Of Biological Chemistry, 2004, v. 279 n. 37, p. 39094-39104en_HK
dc.identifier.issn0021-9258en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91901-
dc.description.abstractBy using single wavelength anomalous diffraction phasing based on the anomalous signal from copper atoms, the crystal structure of atratoxin was determined at the resolution of 1.5 Å and was refined to an ultrahigh resolution of 0.87 Å. The ultrahigh resolution electron density maps allowed the modeling of 38 amino acid residues in alternate conformations and the location of 322 of 870 possible hydrogen atoms. To get accurate information at the atomic level, atratosin-b (an analog of atratoxin with reduced toxicity) was also refined to an atomic resolution of 0.92 Å. By the sequence and structural comparison of these two atratoxins, Arg33 and Arg 36 were identified to be critical to their varied toxicity. The effect of copper ions on the distribution of hydrogen atoms in atratoxin was discussed, and the interactions between copper ions and protein residues were analyzed based on a statistical method, revealing a novel pentahedral copper-binding motif.en_HK
dc.languageengen_HK
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_HK
dc.relation.ispartofJournal of Biological Chemistryen_HK
dc.titleThe atomic resolution crystal structure of atratoxin determined by single wavelength anomalous diffraction phasingen_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.doi10.1074/jbc.M403863200en_HK
dc.identifier.pmid15252034-
dc.identifier.scopuseid_2-s2.0-4644295855en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-4644295855&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume279en_HK
dc.identifier.issue37en_HK
dc.identifier.spage39094en_HK
dc.identifier.epage39104en_HK
dc.identifier.isiWOS:000223684100125-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLou, X=16024965700en_HK
dc.identifier.scopusauthoridLiu, Q=35215401600en_HK
dc.identifier.scopusauthoridTu, X=7102136743en_HK
dc.identifier.scopusauthoridWang, J=36078440500en_HK
dc.identifier.scopusauthoridTeng, M=7101891754en_HK
dc.identifier.scopusauthoridNiu, L=7101760477en_HK
dc.identifier.scopusauthoridSchuller, DJ=7102716051en_HK
dc.identifier.scopusauthoridHuang, Q=32767462600en_HK
dc.identifier.scopusauthoridHao, Q=7102508868en_HK
dc.identifier.citeulike2942943-

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