5EE2

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

5EE2 の概要

• エントリーDOI: 10.2210/pdb5ee2/pdb
• 関連するPDBエントリー: 5EC6
• 分子名称: Hemoglobin-haptoglobin-utilization protein (2 entities in total)
• 機能のキーワード: outer membrane, lipoprotein, receptor, beta barrel, metal transport
• 由来する生物種: Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16770.38

構造登録者

Wong, C.T.,Hare, S.A. (登録日: 2015-10-22, 公開日: 2015-11-04, 最終更新日: 2024-01-10)

主引用文献

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

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: 26671256
DOI: 10.1038/ncomms10172

実験手法

X-RAY DIFFRACTION (1.95 Å)