4HRV

Crystal Structure of Lipoprotein GNA1162 from Neisseria meningitidis

Summary for 4HRV

• Entry DOI: 10.2210/pdb4hrv/pdb
• Descriptor: Putative lipoprotein GNA1162 (2 entities in total)
• Functional Keywords: duf799, lipid binding protein
• Biological source: Neisseria meningitidis
• Total number of polymer chains: 2
• Total formula weight: 36295.05

Authors

Lin, Z.,Cai, X.,Shen, Y. (deposition date: 2012-10-28, release date: 2013-04-24, Last modification date: 2024-10-09)

Primary citation

Cai, X.,Lu, J.,Wu, Z.,Yang, C.,Xu, H.,Lin, Z.,Shen, Y.
Structure of Neisseria meningitidis lipoprotein GNA1162
Acta Crystallogr.,Sect.F, 69:362-368, 2013

PubMed 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.

PubMed: 23545639
DOI: 10.1107/S1744309113004417

Experimental method

X-RAY DIFFRACTION (1.89 Å)