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Structural analysis of haemoglobin binding by HpuA from the Neisseriaceae family
journal contribution
posted on 2023-06-09, 08:01 authored by Chi T Wong, Yingqi Xu, Akshari Gupta, James A Garnett, Steve J Matthews, Stephen HareThe 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.
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- Published
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- Published version
Journal
Nature CommunicationsISSN
2041-1723Publisher
Nature Publishing GroupExternal DOI
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1Volume
6Page range
1-11Article number
a10172Department affiliated with
- Biochemistry Publications
Full text available
- Yes
Peer reviewed?
- Yes
Legacy Posted Date
2017-09-22First Open Access (FOA) Date
2017-09-22First Compliant Deposit (FCD) Date
2017-09-22Usage metrics
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