5EE2
The crystal structure of the C-terminal beta-barrel of HpuA from Neisseria gonorrhoeae
Summary for 5EE2
| Entry DOI | 10.2210/pdb5ee2/pdb |
| Related | 5EC6 |
| Descriptor | Hemoglobin-haptoglobin-utilization protein (2 entities in total) |
| Functional Keywords | outer membrane, lipoprotein, receptor, beta barrel, metal transport |
| Biological source | Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090) |
| Total number of polymer chains | 1 |
| Total formula weight | 16770.38 |
| Authors | Wong, C.T.,Hare, S.A. (deposition date: 2015-10-22, release date: 2015-11-04, Last modification date: 2024-01-10) |
| Primary citation | Wong, C.T.,Xu, Y.,Gupta, A.,Garnett, J.A.,Matthews, S.J.,Hare, S.A. Structural analysis of haemoglobin binding by HpuA from the Neisseriaceae family. Nat Commun, 6:10172-10172, 2015 Cited by PubMed 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. PubMed: 26671256DOI: 10.1038/ncomms10172 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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