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首页> 外文期刊>Acta crystallographica. Section D, Biological crystallography. >Unravelling the shape and structural assembly of the photosynthetic GAPDH-CP12-PRK complex from Arabidopsis thaliana by small-angle X-ray scattering analysis
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Unravelling the shape and structural assembly of the photosynthetic GAPDH-CP12-PRK complex from Arabidopsis thaliana by small-angle X-ray scattering analysis

机译:解体的形状和结构组装光合GAPDH-CP12-PRK复杂拟南芥小角度x射线散射分析

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摘要

Oxygenic photosynthetic organisms produce sugars through the Calvin-Benson cycle, a metabolism that is tightly linked to the light reactions of photosynthesis and is regulated by different mechanisms, including the formation of protein complexes. Two enzymes of the cycle, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and phosphoribulokinase (PRK), form a supramolecular complex with the regulatory protein CP12 with the formula (GAPDH-CP12(2)-PRK) 2, in which both enzyme activities are transiently inhibited during the night. Small-angle X-ray scattering analysis performed on both the GAPDH-CP12-PRK complex and its components, GAPDH-CP12 and PRK, from Arabidopsis thaliana showed that (i) PRK has an elongated, bent and screwed shape, (ii) the oxidized N-terminal region of CP12 that is not embedded in the GAPDH-CP12 complex prefers a compact conformation and (iii) the interaction of PRK with the N-terminal region of CP12 favours the approach of two GAPDH tetramers. The interaction between the GAPDH tetramers may contribute to the overall stabilization of the GAPDH-CP12-PRK complex, the structure of which is presented here for the first time.
机译:氧光合生物产生糖分通过卡尔文本森循环,新陈代谢这是光反应的紧密联系光合作用和由不同机制,包括蛋白质的形成复合物。glyceraldehyde-3-phosphate脱氢酶(GAPDH)和phosphoribulokinase (PRK),形成一个超分子复杂的监管蛋白质CP12公式(GAPDH-CP12 (2) prk)2,两种酶的活动夜里是暂时性的抑制。小角x射线散射分析在GAPDH-CP12-PRK复杂和它组件,GAPDH-CP12和PRK,从拟南芥芥显示(i) PRK拉长,弯曲和螺旋形状,(ii)的氧化氨基端地区CP12这不是嵌入GAPDH-CP12复杂喜欢紧凑构象和(iii) PRK之间的交互的氨基端地区CP12恩惠两个GAPDH四聚体的方法。GAPDH四聚体之间可能导致的GAPDH-CP12-PRK的整体稳定复杂,这是这里介绍的结构第一次。

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