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Enrichment of Bacterial Lipoproteins and Preparation of N-terminal Lipopeptides for Structural Determination by Mass Spectrometry
10:59

Enrichment of Bacterial Lipoproteins and Preparation of N-terminal Lipopeptides for Structural Determination by Mass Spectrometry

Published on: May 21, 2018

Crystal structure of lipoprotein GNA1946 from Neisseria meningitidis

Xue Yang1, Zhenhua Wu, Xiangyu Wang

  • 1Tianjin Key Laboratory of Protein Science, The College of Life Science, Nankai University, Tianjin, China.

Journal of Structural Biology
|September 8, 2009
PubMed

Insights

GNA1946, a meningococcal outer membrane lipoprotein, binds L-methionine. Its structure provides a foundation for developing a broad-spectrum vaccine against Neisseria meningitidis.

Area of Science:

  • Structural biology
  • Microbiology
  • Vaccine development

Background:

  • Neisseria meningitidis poses a significant threat, necessitating a broad-spectrum vaccine.
  • GNA1946, an outer membrane lipoprotein, is a potential vaccine candidate.
  • GNA1946 is predicted to be a periplasmic receptor in the D-methionine uptake ABC transporter system.

Purpose of the Study:

  • To determine the crystal structure of GNA1946.
  • To elucidate the substrate-binding properties of GNA1946.
  • To assess GNA1946's potential as a vaccine target.

Main Methods:

  • Single-wavelength anomalous dispersion (SAD) method was used to solve the crystal structure of GNA1946.
  • Structural comparison with homologous lipoproteins from other bacterial species.
  • Analysis of substrate binding within the GNA1946 structure.

Main Results:

  • The crystal structure of GNA1946 was determined to a resolution of 2.25 A, revealing a Venus flytrap-like conformation.
  • L-methionine was identified bound in the cleft between the two globular lobes of GNA1946.
  • Despite low sequence similarity, GNA1946 exhibits high structural conservation with other methionine-binding lipoproteins, indicating a conserved substrate-binding framework.

Conclusions:

  • GNA1946 functions as an L-methionine binding lipoprotein in the outer membrane of Neisseria meningitidis.
  • GNA1946 acts as a high-affinity, specific initial receptor for ABC transporters.
  • The determined structure of GNA1946 is a crucial starting point for developing a broad-spectrum meningococcal vaccine.

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