3IR1
Crystal Structure of Lipoprotein GNA1946 from Neisseria meningitidis
Summary for 3IR1
Entry DOI | 10.2210/pdb3ir1/pdb |
Related | 3GXA |
Descriptor | Outer membrane lipoprotein GNA1946, METHIONINE, SULFATE ION, ... (4 entities in total) |
Functional Keywords | gna1946, d-methionine cultured, lipoprotein, protein binding |
Biological source | Neisseria meningitidis |
Total number of polymer chains | 6 |
Total formula weight | 166513.31 |
Authors | |
Primary citation | Yang, 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: 19733245DOI: 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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