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Additional file 1: Figure S1. of Sequence analysis and characterization of pyruvate kinase from Clonorchis sinensis, a 53.1-kDa homopentamer, implicated immune protective efficacy against clonorchiasis

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posted on 2017-11-09, 05:00 authored by Tingjin Chen, Hongye Jiang, Hengchang Sun, Zhizhi Xie, Pengli Ren, Lu Zhao, Huimin Dong, Mengchen Shi, Zhiyue Lv, Zhongdao Wu, Xuerong Li, Xinbing Yu, Yan Huang, Jin Xu
Putative tertiary modelling of CsPK. K+ and Mg2+ ions are shown as grey and black spheres, respectively. The N-terminal domain is shown in black. a Ribbon drawing of superposed structure models of CsHK (darker tone) and truncated TgPK1 (lighter tone). The A, B, and C domains of CsHK are shown in blue, red and green, respectively. The catalytic site at the interface of domains A and B and the allosteric site in domain C are highlighted. b Ribbon representation of F16BP (red stick) binding sites of human PK-M2 (lighter tone). S434, S437 (yellow stick), W482 (magenta stick), and R489 (orange stick), which interact with the phosphate moieties, are indicated. The putative corresponding structure of CsPK (darker tone) is shown in panel c. In the active site signature of PK, I267 and S269 (dark red sticks) are replaced by L205 and A207 (blue-violet sticks) in CsHK. Oxalate is indicated as a ball model. d Ribbon representation of the K+-PK-MgIIoxalate-MgIIATP complex closed active site (rabbit PK-M1). ATP, oxalate, and significant residues are shown as red, magenta, and yellow sticks, respectively. e Ribbon drawing of the superposition between the A domains of CsPK with the closed rabbit PK-M1 in complex with ATP and oxalate (dark and lighter tones, respectively). The corresponding significant residues of CsPK are shown in orange (stick). K+ and Mg2+ ions, ATP and oxalate, are shown for reference, with their positions derived from a superposition with 1A49. f Ribbon drawing of superposed structural models of CsPK (darker tone) and LmPYK-suramin (lighter tone) complexed with glycerol (magenta stick) and suramin (an inhibitor of T. brucei glycolytic enzymes, red stick). g Enlargement of the active site of the LmPYK-suramin structure. Significant residues are coloured yellow (stick). The putative corresponding structure of CsPK is shown in panel h. The corresponding significant residues of CsPK are coloured orange (stick). (TIFF 2964 kb)

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the national key research and development program of China

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