Crystal structure of the protein At3g01520, a eukaryotic universal stress protein-like protein from arabidopsis thaliana in complex with AMP

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dc.citation.firstpage1368en_US
dc.citation.issueNumber7en_US
dc.citation.journalTitleProteins: Structure, Function, and Bioinformaticsen_US
dc.citation.lastpage1373en_US
dc.citation.volumeNumber83en_US
dc.contributor.authorKim, Do Jinen_US
dc.contributor.authorBitto, Eduarden_US
dc.contributor.authorBingman, Craig A.en_US
dc.contributor.authorKim, Hyun-Jungen_US
dc.contributor.authorHan, Byung Wooen_US
dc.contributor.authorPhillips, George N.Jr.en_US
dc.date.accessioned2015-11-09T18:52:18Zen_US
dc.date.available2015-11-09T18:52:18Zen_US
dc.date.issued2015en_US
dc.description.abstractMembers of the universal stress protein (USP) family are conserved in a phylogenetically diverse range of prokaryotes, fungi, protists, and plants and confer abilities to respond to a wide range of environmental stresses. Arabidopsis thaliana contains 44 USP domain-containing proteins, and USP domain is found either in a small protein with unknown physiological function or in an N-terminal portion of a multi-domain protein, usually a protein kinase. Here, we report the first crystal structure of a eukaryotic USP-like protein encoded from the gene At3g01520. The crystal structure of the protein At3g01520 was determined by the single-wavelength anomalous dispersion method and refined to an R factor of 21.8% (Rfree =  26.1%) at 2.5 Å resolution. The crystal structure includes three At3g01520 protein dimers with one AMP molecule bound to each protomer, comprising a Rossmann-like α/β overall fold. The bound AMP and conservation of residues in the ATP-binding loop suggest that the protein At3g01520 also belongs to the ATP-binding USP subfamily members.en_US
dc.identifier.citationKim, Do Jin, Bitto, Eduard, Bingman, Craig A., et al.. "Crystal structure of the protein At3g01520, a eukaryotic universal stress protein-like protein from arabidopsis thaliana in complex with AMP." <i>Proteins: Structure, Function, and Bioinformatics,</i> 83, no. 7 (2015) Wiley: 1368-1373. http://dx.doi.org/10.1002/prot.24821.en_US
dc.identifier.doihttp://dx.doi.org/10.1002/prot.24821en_US
dc.identifier.urihttps://hdl.handle.net/1911/82040en_US
dc.language.isoengen_US
dc.publisherWileyen_US
dc.rightsThis is an open access article under the terms of the Creative Commons Attribution NonCommercial License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes.en_US
dc.rights.urihttp://creativecommons.org/licenses/by-nc/4.0/en_US
dc.subject.keyworduniversal stress proteinen_US
dc.subject.keywordArabidopsis thalianaen_US
dc.subject.keywordAt3g01520en_US
dc.titleCrystal structure of the protein At3g01520, a eukaryotic universal stress protein-like protein from arabidopsis thaliana in complex with AMPen_US
dc.typeJournal articleen_US
dc.type.dcmiTexten_US
dc.type.publicationpublisher versionen_US
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