3V8X

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

3V8X の概要

• エントリーDOI: 10.2210/pdb3v8x/pdb
• 関連するPDBエントリー: 3V83 3V89 3V8U
• 分子名称: 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)
• 機能のキーワード: iron binding protein, transferrin binding protein a, iron binding/scavenging, membrane protein-metal transport complex, membrane protein/metal transport
• 由来する生物種: Neisseria meningitidis serogroup B; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 182683.46

構造登録者

Noinaj, N.,Easley, N.,Buchanan, S.K. (登録日: 2011-12-23, 公開日: 2012-02-29, 最終更新日: 2024-11-27)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.6 Å)