1P4T

Crystal structure of Neisserial surface protein A (NspA)

1P4T の概要

• エントリーDOI: 10.2210/pdb1p4t/pdb
• 分子名称: outer membrane protein NspA, SULFATE ION, PENTAETHYLENE GLYCOL MONODECYL ETHER, ... (5 entities in total)
• 機能のキーワード: beta barrel, outer membrane protein, membrane protein
• 由来する生物種: Neisseria meningitidis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18632.30

構造登録者

Vandeputte-Rutten, L.,Bos, M.P.,Tommassen, J.,Gros, P. (登録日: 2003-04-24, 公開日: 2003-07-22, 最終更新日: 2023-11-15)

主引用文献

Vandeputte-Rutten, L.,Bos, M.P.,Tommassen, J.,Gros, P.
Crystal structure of Neisserial Surface Protein A (NspA), a conserved outer membrane protein with vaccine potential
J.Biol.Chem., 278:24825-24830, 2003

PubMed Abstract: The neisserial surface protein A (NspA) from Neisseria meningitidis is a promising vaccine candidate because it is highly conserved among meningococcal strains and induces bactericidal antibodies. NspA is a homolog of the Opa proteins, which mediate adhesion to host cells. Here, we present the crystal structure of NspA, determined to 2.55-A resolution. NspA forms an eight-stranded antiparallel beta-barrel. The four loops at the extracellular side of the NspA molecule form a long cleft, which contains mainly hydrophobic residues and harbors a detergent molecule, suggesting that the protein might function in the binding of hydrophobic ligands, such as lipids. In addition, the structure provides a starting point for structure-based vaccine design.

PubMed: 12716881
DOI: 10.1074/jbc.M302803200

実験手法

X-RAY DIFFRACTION (2.55 Å)