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3IR1

Crystal Structure of Lipoprotein GNA1946 from Neisseria meningitidis

Summary for 3IR1
Entry DOI10.2210/pdb3ir1/pdb
Related3GXA
DescriptorOuter membrane lipoprotein GNA1946, METHIONINE, SULFATE ION, ... (4 entities in total)
Functional Keywordsgna1946, d-methionine cultured, lipoprotein, protein binding
Biological sourceNeisseria meningitidis
Total number of polymer chains6
Total formula weight166513.31
Authors
Yang, X.,Wu, Z.,Wang, X.,Shen, Y. (deposition date: 2009-08-21, release date: 2009-10-13, Last modification date: 2023-11-01)
Primary citationYang, X.,Wu, Z.,Wang, X.,Yang, C.,Xu, H.,Shen, Y.
Crystal structure of lipoprotein GNA1946 from Neisseria meningitidis
J.Struct.Biol., 168:437-443, 2009
Cited by
PubMed Abstract: GNA1946, a conserved outer membrane lipoprotein from Neisseria meningitidis, has been identified as a candidate antigen for an urgently needed broad-spectrum meningococcal vaccine. It has been predicted to be a periplasmic receptor in the D-methionine uptake ABC transporter system. The crystal structure of GNA1946 was solved by the single-wavelength anomalous dispersion (SAD) method to a resolution of 2.25 A, and it reveals a Venus flytrap-like structure. GNA1946 consists of two globular lobes connected by a hinge region. Surprisingly, the structure showed an L-methionine bound within the cleft between the lobes. A comparison of GNA1946 with two other outer membrane lipoproteins, the L-methionine-binding Tp32 from Treponema pallidum and the dipeptide GlyMet-binding protein Pg110 from Staphylococcus aureus, revealed that although these three proteins share low sequence similarities, there is a high degree of structural conservation and similar substrate-binding frameworks. Our results reveal that GNA1946 is an L-methionine binding lipoprotein in the outer membrane, and should function as an initial receptor for ABC transporters with high affinity and specificity. The GNA1946 structure reported here should provide a valuable starting point for the development of a broad-spectrum meningococcal vaccine.
PubMed: 19733245
DOI: 10.1016/j.jsb.2009.09.001
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.15 Å)
Structure validation

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