Search

Your search keyword '"Jeffrey Y. Lai"' showing total 2 results
Start Over Author "Jeffrey Y. Lai" Language english
2 results on '"Jeffrey Y. Lai"'

1. Characterization of the ABC methionine transporter from Neisseria meningitidis reveals that lipidated MetQ is required for interaction

Author

Naima G Sharaf, Mona Shahgholi, Esther Kim, Jeffrey Y Lai, David G VanderVelde, Allen T Lee, and Douglas C Rees

Subjects
lipoprotein, ABC transporters, Neisseria meningitidis, methionine importers, single particle cryoem, fluorine solution nmr, Medicine, Science, Biology (General), QH301-705.5
Abstract

NmMetQ is a substrate-binding protein (SBP) from Neisseria meningitidis that has been identified as a surface-exposed candidate antigen for meningococcal vaccines. However, this location for NmMetQ challenges the prevailing view that SBPs in Gram-negative bacteria are localized to the periplasmic space to promote interaction with their cognate ABC transporter embedded in the bacterial inner membrane. To elucidate the roles of NmMetQ, we characterized NmMetQ with and without its cognate ABC transporter (NmMetNI). Here, we show that NmMetQ is a lipoprotein (lipo-NmMetQ) that binds multiple methionine analogs and stimulates the ATPase activity of NmMetNI. Using single-particle electron cryo-microscopy, we determined the structures of NmMetNI in the presence and absence of lipo-NmMetQ. Based on our data, we propose that NmMetQ tethers to membranes via a lipid anchor and has dual function and localization, playing a role in NmMetNI-mediated transport at the inner membrane and moonlighting on the bacterial surface.

Published
2021
Full Text
View/download PDF

2. Characterization of the ABC methionine transporter from Neisseria meningitidis reveals that lipidated MetQ is required for interaction

Author

Esther Kim, Allen T. Lee, Douglas C. Rees, Jeffrey Y. Lai, Mona Shahgholi, David G. VanderVelde, and Naima G. Sharaf

Subjects
fluorine solution nmr, methionine importers, QH301-705.5, Structural Biology and Molecular Biophysics, Lipoproteins, Science, Chemical biology, ATP-binding cassette transporter, Neisseria meningitidis, medicine.disease_cause, General Biochemistry, Genetics and Molecular Biology, Protein Structure, Secondary, chemistry.chemical_compound, Methionine, Bacterial Proteins, Biochemistry and Chemical Biology, medicine, Inner membrane, Amino Acid Sequence, Biology (General), General Immunology and Microbiology, biology, Chemistry, General Neuroscience, Cryoelectron Microscopy, lipoprotein, E. coli, General Medicine, Periplasmic space, biology.organism_classification, Cell biology, Protein Structure, Tertiary, single particle cryoem, Structural biology, ABC transporters, Periplasm, Medicine, ATP-Binding Cassette Transporters, Bacteria, Research Article, Protein Binding
Abstract

NmMetQ is a substrate-binding protein (SBP) from Neisseria meningitidis that has been identified as a surface-exposed candidate antigen for meningococcal vaccines. However, this location for NmMetQ challenges the prevailing view that SBPs in Gram-negative bacteria are localized to the periplasmic space to promote interaction with their cognate ABC transporter embedded in the bacterial inner membrane. To elucidate the roles of NmMetQ, we characterized NmMetQ with and without its cognate ABC transporter (NmMetNI). Here, we show that NmMetQ is a lipoprotein (lipo-NmMetQ) that binds multiple methionine analogs and stimulates the ATPase activity of NmMetNI. Using single-particle electron cryo-microscopy, we determined the structures of NmMetNI in the presence and absence of lipo-NmMetQ. Based on our data, we propose that NmMetQ tethers to membranes via a lipid anchor and has dual function and localization, playing a role in NmMetNI-mediated transport at the inner membrane and moonlighting on the bacterial surface.

Published
2021

Catalog

Books, media, physical & digital resources
See catalog results