8CHX
Structure and function of LolA from Vibrio cholerae
Summary for 8CHX
Entry DOI | 10.2210/pdb8chx/pdb |
Descriptor | Outer-membrane lipoprotein carrier protein, ZINC ION (3 entities in total) |
Functional Keywords | lipid, periplasm, gram-negative, lipid transport |
Biological source | Vibrio cholerae |
Total number of polymer chains | 2 |
Total formula weight | 48036.65 |
Authors | Jaiman, D.,Nagampalli, R.,Persson, K. (deposition date: 2023-02-08, release date: 2023-06-21, Last modification date: 2024-06-19) |
Primary citation | Jaiman, D.,Nagampalli, R.,Persson, K. A comparative analysis of lipoprotein transport proteins: LolA and LolB from Vibrio cholerae and LolA from Porphyromonas gingivalis. Sci Rep, 13:6605-6605, 2023 Cited by PubMed Abstract: In Gram-negative bacteria, N-terminal lipidation is a signal for protein trafficking from the inner membrane (IM) to the outer membrane (OM). The IM complex LolCDE extracts lipoproteins from the membrane and moves them to the chaperone LolA. The LolA-lipoprotein complex crosses the periplasm after which the lipoprotein is anchored to the OM. In γ-proteobacteria anchoring is assisted by the receptor LolB, while a corresponding protein has not been identified in other phyla. In light of the low sequence similarity between Lol-systems from different phyla and that they may use different Lol components, it is crucial to compare representative proteins from several species. Here we present a structure-function study of LolA and LolB from two phyla: LolA from Porphyromonas gingivalis (phylum bacteroidota), and LolA and LolB from Vibrio cholerae (phylum proteobacteria). Despite large sequence differences, the LolA structures are very similar, hence structure and function have been conserved throughout evolution. However, an Arg-Pro motif crucial for function in γ-proteobacteria has no counterpart in bacteroidota. We also show that LolA from both phyla bind the antibiotic polymyxin B whereas LolB does not. Collectively, these studies will facilitate the development of antibiotics as they provide awareness of both differences and similarities across phyla. PubMed: 37095149DOI: 10.1038/s41598-023-33705-y PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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