1p4t
From Proteopedia
Crystal structure of Neisserial surface protein A (NspA)
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Crystal structure of Neisserial surface protein A (NspA), a conserved outer membrane protein with vaccine potential.,Vandeputte-Rutten L, Bos MP, Tommassen J, Gros P J Biol Chem. 2003 Jul 4;278(27):24825-30. Epub 2003 Apr 26. PMID:12716881[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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