The crystal structure of HpuA from Kingella denitrificans in complex with human haemoglobinThe crystal structure of HpuA from Kingella denitrificans in complex with human haemoglobin

Structural highlights

5ee4 is a 6 chain structure with sequence from Homo sapiens and Kingella denitrificans ATCC 33394. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

F0EX68_9NEIS

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.

See Also

References

  1. 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

5ee4, resolution 2.30Å

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