Structural analysis of haemoglobin binding by HpuA from the Neisseriaceae family

Wong, Chi T, Xu, Yingqi, Gupta, Akshari, Garnett, James A, Matthews, Steve J and Hare, Stephen A (2015) Structural analysis of haemoglobin binding by HpuA from the Neisseriaceae family. Nature Communications, 6 (1). a10172 1-11. ISSN 2041-1723

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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.

Item Type: Article
Schools and Departments: School of Life Sciences > Biochemistry
Depositing User: Stephen Hare
Date Deposited: 22 Sep 2017 08:05
Last Modified: 14 Aug 2020 09:45

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