5ee2

The crystal structure of the C-terminal beta-barrel of HpuA from Neisseria gonorrhoeae

spinqualitylabelsall models 5ee2, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ee2 is a 1 chain structure with sequence from Neisseria gonorrhoeae FA 1090. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.95Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0H4IWK3_NEIG1 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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