8CHX
Structure and function of LolA from Vibrio cholerae
8CHX の概要
| エントリーDOI | 10.2210/pdb8chx/pdb |
| 分子名称 | Outer-membrane lipoprotein carrier protein, ZINC ION (3 entities in total) |
| 機能のキーワード | lipid, periplasm, gram-negative, lipid transport |
| 由来する生物種 | Vibrio cholerae |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 48036.65 |
| 構造登録者 | |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.8 Å) |
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