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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >pH-dependent structural changes in haemoglobin component V from the midge larva Propsilocerus akamusi (Orthocladiinae, Diptera).
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pH-dependent structural changes in haemoglobin component V from the midge larva Propsilocerus akamusi (Orthocladiinae, Diptera).

机译：pH-dependent血红蛋白的结构变化组件从蚊幼虫Propsilocerus V

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摘要

Haemoglobin component V (Hb V) from the midge larva Propsilocerus akamusi exhibits oxygen affinity despite the replacement of HisE7 and a pH-dependence of its functional properties. In order to understand the contribution of the distal residue to the ligand-binding properties and the pH-dependent structural changes in this insect Hb, the crystal structure of Hb V was determined under five different pH conditions. Structural comparisons of these Hb structures indicated that at neutral pH ArgE10 contributes to the stabilization of the haem-bound ligand molecule as a functional substitute for the nonpolar E7 residue. However, ArgE10 does not contribute to stabilization at acidic and alkaline pH because of the swinging movement of the Arg side chain under these conditions. This pH-dependent behaviour of Arg results in significant differences in the hydrogen-bond network on the distal side of the haem in the Hb V structures at different pH values. Furthermore, the change in pH results in a partial movement of the F helix, considering that coupled movements of ArgE10 and the F helix determine the haem location at each pH. These results suggested that Hb V retains its functional properties by adapting to the structural changes caused by amino-acid replacements.
机译：血红蛋白从蚊组件V (Hb V)幼虫Propsilocerus akamusi展品氧气亲和力尽管HisE7和替换pH-dependence其功能性质。为了理解的贡献远端残留的配体结合的属性和pH-dependent结构性变化昆虫Hb, Hb V的晶体结构在五个不同的pH值条件下决定。结构比较这些Hb结构表明在中性pH ArgE10贡献haem-bound配体的稳定分子功能的替代品非极性E7残渣。导致在酸性和稳定性碱性pH值的摆动运动在这些条件下参数的侧链。pH-dependent参数导致的行为形成氢键的显著差异网络的远端一侧Hb的血红素V结构在不同的pH值。pH值的变化导致部分的运动F螺旋,考虑耦合的运动ArgE10和F螺旋确定血红素位置在每个博士认为这些结果Hb V保留其功能性质适应造成的结构性变化氨基酸替换。

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