Back to Search
Start Over
Crystal structure of lipoprotein GNA1946 from Neisseria meningitidis
- Source :
-
Journal of Structural Biology . Dec2009, Vol. 168 Issue 3, p437-443. 7p. - Publication Year :
- 2009
-
Abstract
- 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 2.25Å, 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. [Copyright &y& Elsevier]
Details
- Language :
- English
- ISSN :
- 10478477
- Volume :
- 168
- Issue :
- 3
- Database :
- Academic Search Index
- Journal :
- Journal of Structural Biology
- Publication Type :
- Academic Journal
- Accession number :
- 44935124
- Full Text :
- https://doi.org/10.1016/j.jsb.2009.09.001