3V8X

The crystal structure of transferrin binding protein A (TbpA) from Neisserial meningitidis serogroup B in complex with full length human transferrin

Summary for 3V8X

• Entry DOI: 10.2210/pdb3v8x/pdb
• Related: 3V83 3V89 3V8U
• Descriptor: Transferrin-binding protein 1, Serotransferrin, N-acetyl-alpha-neuraminic acid-(2-6)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-alpha-D-mannopyranose-(1-3)-[beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: iron binding protein, transferrin binding protein a, iron binding/scavenging, membrane protein-metal transport complex, membrane protein/metal transport
• Biological source: Neisseria meningitidis serogroup B; More
• Total number of polymer chains: 2
• Total formula weight: 182683.46

Authors

Noinaj, N.,Easley, N.,Buchanan, S.K. (deposition date: 2011-12-23, release date: 2012-02-29, Last modification date: 2024-11-27)

Primary citation

Noinaj, N.,Easley, N.C.,Oke, M.,Mizuno, N.,Gumbart, J.,Boura, E.,Steere, A.N.,Zak, O.,Aisen, P.,Tajkhorshid, E.,Evans, R.W.,Gorringe, A.R.,Mason, A.B.,Steven, A.C.,Buchanan, S.K.
Structural basis for iron piracy by pathogenic Neisseria.
Nature, 483:53-58, 2012

PubMed Abstract: Neisseria are obligate human pathogens causing bacterial meningitis, septicaemia and gonorrhoea. Neisseria require iron for survival and can extract it directly from human transferrin for transport across the outer membrane. The transport system consists of TbpA, an integral outer membrane protein, and TbpB, a co-receptor attached to the cell surface; both proteins are potentially important vaccine and therapeutic targets. Two key questions driving Neisseria research are how human transferrin is specifically targeted, and how the bacteria liberate iron from transferrin at neutral pH. To address these questions, we solved crystal structures of the TbpA-transferrin complex and of the corresponding co-receptor TbpB. We characterized the TbpB-transferrin complex by small-angle X-ray scattering and the TbpA-TbpB-transferrin complex by electron microscopy. Our studies provide a rational basis for the specificity of TbpA for human transferrin, show how TbpA promotes iron release from transferrin, and elucidate how TbpB facilitates this process.

PubMed: 22327295
DOI: 10.1038/nature10823

Experimental method

X-RAY DIFFRACTION (2.6 Å)