PDBsum entry 5ec6

Metal transport

PDB id: 5ec6

Contents

Protein chain

302 a.a.

Ligands

GOL ×2

Waters ×325

PDB id:

5ec6

Name:

Metal transport

Title:

The apo crystal structure of haemoglobin receptor hpua from kingella denitrificans

Structure:

Hpua. Chain: a. Engineered: yes

Source:

Kingella denitrificans atcc 33394. Organism_taxid: 888741. Atcc: 33394. Gene: hmpref9098_0447. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.60Å R-factor: 0.172 R-free: 0.196

Authors:

C.T.Wong,J.A.Garnett,S.A.Hare

Key ref:

C.T.Wong et al. (2015). Structural analysis of haemoglobin binding by HpuA from the Neisseriaceae family. Nat Commun, 6, 10172. PubMed id: 26671256 DOI: 10.1038/ncomms10172

Date:

20-Oct-15 Release date: 04-Nov-15

Protein chain

F0EX68  (F0EX68_9NEIS) -  Transferrin-binding protein B C-lobe/N-lobe beta barrel domain-containing protein from Kingella denitrificans ATCC 33394

Seq: 340 a.a.

Struc: 302 a.a.

DOI no: 10.1038/ncomms10172

Nat Commun 6:10172 (2015)

PubMed id: 26671256

Structural analysis of haemoglobin binding by HpuA from the Neisseriaceae family.

C.T.Wong, Y.Xu, A.Gupta, J.A.Garnett, S.J.Matthews, S.A.Hare.

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.