Structural highlights
Publication Abstract from PubMed
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.
Structural analysis of haemoglobin binding by HpuA from the Neisseriaceae family.,Wong CT, Xu Y, Gupta A, Garnett JA, Matthews SJ, Hare SA Nat Commun. 2015 Dec 16;6:10172. doi: 10.1038/ncomms10172. PMID:26671256[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wong CT, Xu Y, Gupta A, Garnett JA, Matthews SJ, Hare SA. Structural analysis of haemoglobin binding by HpuA from the Neisseriaceae family. Nat Commun. 2015 Dec 16;6:10172. doi: 10.1038/ncomms10172. PMID:26671256 doi:http://dx.doi.org/10.1038/ncomms10172
