4QQ1
Crystal structure of the isotype 1 Transferrin binding protein B (TbpB) from serogroup B Neisseria meningitidis
4QQ1 の概要
| エントリーDOI | 10.2210/pdb4qq1/pdb |
| 分子名称 | Transferrin-binding protein 2, CESIUM ION, GLYCEROL, ... (5 entities in total) |
| 機能のキーワード | vaccine candidate, transferrin receptor, iron acquisition, surface lipoprotein, host-pathogen interaction, iron piracy, transferrin binding, outer-membrane, protein binding |
| 由来する生物種 | Neisseria meningitidis serogroup B |
| 細胞内の位置 | Cell outer membrane ; Lipid- anchor : Q06988 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 179713.31 |
| 構造登録者 | |
| 主引用文献 | Adamiak, P.,Calmettes, C.,Moraes, T.F.,Schryvers, A.B. Patterns of structural and sequence variation within isotype lineages of the Neisseria meningitidis transferrin receptor system. Microbiologyopen, 4:491-504, 2015 Cited by PubMed Abstract: Neisseria meningitidis inhabits the human upper respiratory tract and is an important cause of sepsis and meningitis. A surface receptor comprised of transferrin-binding proteins A and B (TbpA and TbpB), is responsible for acquiring iron from host transferrin. Sequence and immunological diversity divides TbpBs into two distinct lineages; isotype I and isotype II. Two representative isotype I and II strains, B16B6 and M982, differ in their dependence on TbpB for in vitro growth on exogenous transferrin. The crystal structure of TbpB and a structural model for TbpA from the representative isotype I N. meningitidis strain B16B6 were obtained. The structures were integrated with a comprehensive analysis of the sequence diversity of these proteins to probe for potential functional differences. A distinct isotype I TbpA was identified that co-varied with TbpB and lacked sequence in the region for the loop 3 α-helix that is proposed to be involved in iron removal from transferrin. The tightly associated isotype I TbpBs had a distinct anchor peptide region, a distinct, smaller linker region between the lobes and lacked the large loops in the isotype II C-lobe. Sequences of the intact TbpB, the TbpB N-lobe, the TbpB C-lobe, and TbpA were subjected to phylogenetic analyses. The phylogenetic clustering of TbpA and the TbpB C-lobe were similar with two main branches comprising the isotype 1 and isotype 2 TbpBs, possibly suggesting an association between TbpA and the TbpB C-lobe. The intact TbpB and TbpB N-lobe had 4 main branches, one consisting of the isotype 1 TbpBs. One isotype 2 TbpB cluster appeared to consist of isotype 1 N-lobe sequences and isotype 2 C-lobe sequences, indicating the swapping of N-lobes and C-lobes. Our findings should inform future studies on the interaction between TbpB and TbpA and the process of iron acquisition. PubMed: 25800619DOI: 10.1002/mbo3.254 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.33 Å) |
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