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2LC4

Solution Structure of PilP from Pseudomonas aeruginosa

2LC4 の概要
エントリーDOI10.2210/pdb2lc4/pdb
NMR情報BMRB: 17598
分子名称PilP protein (1 entity in total)
機能のキーワードtype iv pilus, structural protein
由来する生物種Pseudomonas aeruginosa
タンパク質・核酸の鎖数1
化学式量合計12427.05
構造登録者
Howell, P.,Tammam, S.,Chong, P.,Forman-Kay, J.D. (登録日: 2011-04-22, 公開日: 2011-12-21, 最終更新日: 2024-05-15)
主引用文献Tammam, S.,Sampaleanu, L.M.,Koo, J.,Sundaram, P.,Ayers, M.,Andrew Chong, P.,Forman-Kay, J.D.,Burrows, L.L.,Howell, P.L.
Characterization of the PilN, PilO and PilP type IVa pilus subcomplex.
Mol.Microbiol., 82:1496-1514, 2011
Cited by
PubMed Abstract: Type IVa pili are bacterial nanomachines required for colonization of surfaces, but little is known about the organization of proteins in this system. The Pseudomonas aeruginosa pilMNOPQ operon encodes five key members of the transenvelope complex facilitating pilus function. While PilQ forms the outer membrane secretin pore, the functions of the inner membrane-associated proteins PilM/N/O/P are less well defined. Structural characterization of a stable C-terminal fragment of PilP (PilP(Δ71)) by NMR revealed a modified β-sandwich fold, similar to that of Neisseria meningitidis PilP, although complementation experiments showed that the two proteins are not interchangeable likely due to divergent surface properties. PilP is an inner membrane putative lipoprotein, but mutagenesis of the putative lipobox had no effect on the localization and function of PilP. A larger fragment, PilP(Δ18-6His), co-purified with a PilN(Δ44)/PilO(Δ51) heterodimer as a stable complex that eluted from a size exclusion chromatography column as a single peak with a molecular weight equivalent to two heterotrimers with 1:1:1 stoichiometry. Although PilO forms both homodimers and PilN-PilO heterodimers, PilP(Δ18-6His) did not interact stably with PilO(Δ51) alone. Together these data demonstrate that PilN/PilO/PilP interact directly to form a stable heterotrimeric complex, explaining the dispensability of PilP's lipid anchor for localization and function.
PubMed: 22053789
DOI: 10.1111/j.1365-2958.2011.07903.x
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2lc4
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-11-20に公開中

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