1P4T
Crystal structure of Neisserial surface protein A (NspA)
Summary for 1P4T
| Entry DOI | 10.2210/pdb1p4t/pdb |
| Descriptor | outer membrane protein NspA, SULFATE ION, PENTAETHYLENE GLYCOL MONODECYL ETHER, ... (5 entities in total) |
| Functional Keywords | beta barrel, outer membrane protein, membrane protein |
| Biological source | Neisseria meningitidis |
| Total number of polymer chains | 1 |
| Total formula weight | 18632.30 |
| Authors | Vandeputte-Rutten, L.,Bos, M.P.,Tommassen, J.,Gros, P. (deposition date: 2003-04-24, release date: 2003-07-22, Last modification date: 2023-11-15) |
| Primary citation | 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 Cited by 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: 12716881DOI: 10.1074/jbc.M302803200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.55 Å) |
Structure validation
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