Literature DB >> 23545639

Structure of Neisseria meningitidis lipoprotein GNA1162.

Xiangyu Cai1, Jing Lu, Zhenhua Wu, Chunting Yang, Honglin Xu, Zhijie Lin, Yuequan Shen.   

Abstract

GNA1162, a predicted lipoprotein from Neisseria meningitidis, is a potential candidate for a universal vaccine against meningococcal disease caused by N. meningitidis serogroup B. Here, the crystal structure of GNA1162 at 1.89 Å resolution determined by single-wavelength anomalous dispersion (SAD) is reported. The structure of GNA1162 appears to be a dimer in the crystallographic asymmetric unit as well as in solution. The overall structure of the dimer indicates that each monomer inserts its C-terminal α5 helix into the hydrophobic groove of the other molecule. Moreover, the β4 strands of each monomer lie antiparallel to each other and interact through multiple main-chain hydrogen bonds. Through structural comparisons and operon predictions, it is hypothesized that GNA1162 is part of a transport system and assists in transport and reassembly. The crystal structure of GNA1162 sheds light on its possible function and provides potentially valuable information for the design of a vaccine against meningococcal disease.

Entities:  

Keywords:  GNA1162; lipoproteins; outer membrane proteins; transport systems

Mesh:

Substances:

Year:  2013        PMID: 23545639      PMCID: PMC3614158          DOI: 10.1107/S1744309113004417

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


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