Structural and biochemical characterization of the cytosolic wheat cyclophilin TaCypA-1 = 빵밀유래 시토졸 시클로필린TaCypA-1의 구조 및 생화학적 특성

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dc.contributor.authorS S Sekhon-
dc.contributor.authorH Kaur-
dc.contributor.authorT Dutta-
dc.contributor.authorK Singh-
dc.contributor.authorS Kumari-
dc.contributor.authorSunghyun Kang-
dc.contributor.authorSung Goo Park-
dc.contributor.authorByoung Chul Park-
dc.contributor.authorDae Gwin Jeong-
dc.contributor.authorA Pareek-
dc.contributor.authorEui-jeon Woo-
dc.contributor.authorP Singh-
dc.contributor.authorTae-Sung Yoon-
dc.date.accessioned2017-04-19T09:37:50Z-
dc.date.available2017-04-19T09:37:50Z-
dc.date.issued2013-
dc.identifier.citationActa Crystallographica. Section D, Biological Crystallography,69,4,555,563ko
dc.identifier.issn0907-4449-
dc.identifier.uri10.1107/S0907444912051529ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/11256-
dc.description.abstractCyclophilins belong to a family of proteins that bind to the immunosuppressive drug cyclosporin A (CsA). Several members of this protein family catalyze the cis-trans isomerization of peptide bonds preceding prolyl residues. The present study describes the biochemical and structural characteristics of a cytosolic cyclophilin (TaCypA-1) cloned from wheat (Triticum aestivum L.). Purified TaCypA-1 expressed in Escherichia coli showed peptidyl-prolyl cis-trans isomerase activity, which was inhibited by CsA with an inhibition constant of 78.3nM. The specific activity and catalytic efficiency (k cat/K m) of the purified TaCypA-1 were 99.06 ± 0.13nmols -1mg-1 and 2.32 × 105 M -1s-1, respectively. The structures of apo TaCypA-1 and the TaCypA-1-CsA complex were determined at 1.25 and 1.20A resolution, respectively, using X-ray diffraction. Binding of CsA to the active site of TaCypA-1 did not result in any significant conformational change in the apo TaCypA-1 structure. This is consistent with the crystal structure of the human cyclophilin D-CsA complex reported at 0.96A resolution. The TaCypA-1 structure revealed the presence of a divergent loop of seven amino acids 48KSGKPLH54 which is a characteristic feature of plant cyclophilins. This study is the first to elucidate the structure of an enzymatically active plant cyclophilin which shows peptidyl-prolyl cis-trans isomerase activity and the presence of a divergent loop.-
dc.publisherInt Union Crystallography-
dc.titleStructural and biochemical characterization of the cytosolic wheat cyclophilin TaCypA-1 = 빵밀유래 시토졸 시클로필린TaCypA-1의 구조 및 생화학적 특성-
dc.title.alternativeStructural and biochemical characterization of the cytosolic wheat cyclophilin TaCypA-1-
dc.typeArticle-
dc.citation.titleActa Crystallographica Section D-Biological Crystallography-
dc.citation.number4-
dc.citation.endPage563-
dc.citation.startPage555-
dc.citation.volume69-
dc.contributor.affiliatedAuthorSunghyun Kang-
dc.contributor.affiliatedAuthorSung Goo Park-
dc.contributor.affiliatedAuthorByoung Chul Park-
dc.contributor.affiliatedAuthorDae Gwin Jeong-
dc.contributor.affiliatedAuthorEui-jeon Woo-
dc.contributor.affiliatedAuthorTae-Sung Yoon-
dc.contributor.alternativeNameSekhon-
dc.contributor.alternativeNameKaur-
dc.contributor.alternativeNameDutta-
dc.contributor.alternativeNameSingh-
dc.contributor.alternativeNameKumari-
dc.contributor.alternativeName강성현-
dc.contributor.alternativeName박성구-
dc.contributor.alternativeName박병철-
dc.contributor.alternativeName정대균-
dc.contributor.alternativeNamePareek-
dc.contributor.alternativeName우의전-
dc.contributor.alternativeNameSingh-
dc.contributor.alternativeName윤태성-
dc.identifier.bibliographicCitationActa Crystallographica Section D-Biological Crystallography, vol. 69, no. 4, pp. 555-563-
dc.identifier.doi10.1107/S0907444912051529-
dc.subject.keywordcyclophilins-
dc.subject.keywordpeptidyl-prolyl cis-trans isomerase-
dc.subject.keywordTriticum aestivum-
dc.subject.localCyclophilin-
dc.subject.localcyclophilins-
dc.subject.localpeptidyl-prolyl cis-trans isomerase-
dc.subject.localpeptidyl-prolyl cis/trans-isomerase-
dc.subject.localPeptidyl prolyl cis/trans isomerase-
dc.subject.localTriticum aestivum L.-
dc.subject.localTriticum aestivum L-
dc.subject.localTriticum aestivum-
dc.description.journalClassY-
Appears in Collections:
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
Division of Research on National Challenges > Bionanotechnology Research Center > 1. Journal Articles
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