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Structural analysis of haemoglobin binding by HpuA from the Neisseriaceae family

DOI: 10.1038/ncomms10172 DOI Help
PMID: 26671256 PMID Help

Authors: Chi T. Wong (Imperial College London) , Yingqi Xu (Imperial College London) , Akshari Gupta (Imperial College London) , James A. Garnett (Imperial College London) , Steve J. Matthews (Imperial College London) , Stephen A. Hare (Imperial College London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 6

State: Published (Approved)
Published: December 2015

Open Access Open Access

Abstract: 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

Journal Keywords: Microbiology; Biochemistry

Diamond Keywords: Bacteria

Subject Areas: Biology and Bio-materials, Chemistry

Instruments: I04-1-Macromolecular Crystallography (fixed wavelength) , I04-Macromolecular Crystallography

Added On: 05/01/2016 12:56


Discipline Tags:

Pathogens Infectious Diseases Health & Wellbeing Biochemistry Chemistry Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)