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Title 

Structural and biochemical characterization of the cytosolic wheat cyclophilin TaCypA-1

 

빵밀유래 시토졸 시클로필린TaCypA-1의 구조 및 생화학적 특성

Authors 

S S SekhonH KaurT DuttaK SinghS KumariSunghyun KangSung Goo ParkByoung Chul ParkDae Gwin JeongA PareekEui-jeon WooP SinghTae-Sung Yoon

Publisher 

International Union of Crystallography

Issue Date 

2013

Citation 

Acta Crystallographica. Section D, Biological Crystallography, vol. 69, no. 4, pp. 555-563

Keywords 

cyclophilinspeptidyl-prolyl cis-trans isomeraseTriticum aestivum

Abstract 

Cyclophilins 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 1.20? 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 0.96? 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.

Citation 

Acta Crystallographica. Section D, Biological Crystallography, 69(4): 555-563

ISSN 

0907-4449

Link 

http://dx.doi.org/10.1107/S0907444912051529

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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