4RVW

Structure of the bacterial Zn-transporter ZnuD from Neisseria meningitidis (soaked with 20 micromolar Zinc)

Summary for 4RVW

• Entry DOI: 10.2210/pdb4rvw/pdb
• Descriptor: ZnuD, ZINC ION, SULFATE ION (3 entities in total)
• Functional Keywords: outer membrane protein, zinc transporter, zinc acquisition, tonb dependant receptor, vaccine candidate, transport protein
• Biological source: Neisseria meningitidis MC58
• Cellular location: Cell outer membrane : Q9JZN9
• Total number of polymer chains: 1
• Total formula weight: 84626.97

Authors

Calmettes, C.,Moraes, T.F. (deposition date: 2014-11-28, release date: 2015-08-19, Last modification date: 2024-02-28)

Primary citation

Calmettes, C.,Ing, C.,Buckwalter, C.M.,El Bakkouri, M.,Chieh-Lin Lai, C.,Pogoutse, A.,Gray-Owen, S.D.,Pomes, R.,Moraes, T.F.
The molecular mechanism of Zinc acquisition by the neisserial outer-membrane transporter ZnuD.
Nat Commun, 6:7996-7996, 2015

PubMed Abstract: Invading bacteria from the Neisseriaceae, Acinetobacteriaceae, Bordetellaceae and Moraxellaceae families express the conserved outer-membrane zinc transporter zinc-uptake component D (ZnuD) to overcome nutritional restriction imposed by the host organism during infection. Here we demonstrate that ZnuD is required for efficient systemic infections by the causative agent of bacterial meningitis, Neisseria meningitidis, in a mouse model. We also combine X-ray crystallography and molecular dynamics simulations to gain insight into the mechanism of zinc recognition and transport across the bacterial outer-membrane by ZnuD. Because ZnuD is also considered a promising vaccine candidate against N. meningitidis, we use several ZnuD structural intermediates to map potential antigenic epitopes, and propose a mechanism by which ZnuD can maintain high sequence conservation yet avoid immune recognition by altering the conformation of surface-exposed loops.

PubMed: 26282243
DOI: 10.1038/ncomms8996

Experimental method

X-RAY DIFFRACTION (4.477 Å)