Structural analysis of haemoglobin binding by HpuA from the Neisseriaceae family.,Nature Communications

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Structural analysis of haemoglobin binding by HpuA from the Neisseriaceae family.
Nature Communications ( IF 14.7 ) Pub Date : 2015-Dec-16 , DOI: 10.1038/ncomms10172
Chi T Wong ₁ , Yingqi Xu ₁ , Akshari Gupta ₁ , James A Garnett ₁ , Steve J Matthews ₁ , Stephen A Hare ₁

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The Neisseriaceae family of bacteria causes a range of diseases including meningitis, septicaemia, gonorrhoea and endocarditis, and extracts haem from haemoglobin as an important iron source within the iron-limited environment of its human host. Herein we report crystal structures of apo- and haemoglobin-bound HpuA, an essential component of this haem import system. The interface involves long loops on the bacterial receptor that present hydrophobic side chains for packing against the surface of haemoglobin. Interestingly, our structural and biochemical analyses of Kingella denitrificans and Neisseria gonorrhoeae HpuA mutants, although validating the interactions observed in the crystal structure, show how Neisseriaceae have the fascinating ability to diversify functional sequences and yet retain the haemoglobin binding function. Our results present the first description of HpuA's role in direct binding of haemoglobin.

中文翻译：

奈瑟菌科 HpuA 结合血红蛋白的结构分析。

奈瑟菌科细菌引起一系列疾病，包括脑膜炎、败血症、淋病和心内膜炎，并从血红蛋白中提取血红素作为其人类宿主铁限制环境中的重要铁源。在这里，我们报告了载脂蛋白和血红蛋白结合的 HpuA 的晶体结构，这是这种血红素输入系统的重要组成部分。该界面涉及细菌受体上的长环，这些环呈现疏水侧链，用于堆积在血红蛋白表面。有趣的是，我们对 Kingella denitrificans 和 Neisseria gonorrhoeae HpuA 突变体的结构和生化分析，虽然验证了在晶体结构中观察到的相互作用，但显示了 Neisseriaceae 如何具有使功能序列多样化并保留血红蛋白结合功能的迷人能力。

更新日期：2016-01-01

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