8WDF
Chemoreceptor PilJ from Pseudomonas aeruginosa PA14
8WDF の概要
| エントリーDOI | 10.2210/pdb8wdf/pdb |
| 分子名称 | Protein PilJ (1 entity in total) |
| 機能のキーワード | chemoreceptor pilj-lbd, hydrolase |
| 由来する生物種 | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 31476.92 |
| 構造登録者 | |
| 主引用文献 | Cui, R.,Wang, Q.A.,Guo, L.,Li, D.F. The ligand binding domain of a type IV pilus chemoreceptor PilJ has a different fold from that of another PilJ-type receptor McpN. Biochem.Biophys.Res.Commun., 706:149765-149765, 2024 Cited by PubMed Abstract: Bacterial chemoreceptors sense the extracellular signals and regulate bacterial motilities, biofilm formation, etc. The periplasmic ligand binding domains of chemoreceptors occur as different structural folds and recognize a diversity of chemical molecules. In Pseudomonas aeruginosa (PAO1), two bacterial chemoreceptors, McpN (PA2788) and PilJ (PA0411), are proposed to both contain a PilJ-like ligand-binding domain (LBD) (Pfam motif PF13675) and involved in nitrate chemotaxis and type IV pilus-mediated motility, respectively. The LBDs of McpN and PilJ consist of 135 and 263 residues, respectively, and share very low sequence identity, suggesting they might occur as different structures. Here, we found that PilJ-LBD folded into an HBM module, the same as the sensor domains of McpS-LBD and TorS-LBD, but it differed from that of McpN-LBD. We also observed a trimer in SEC and AUC and proposed a trimeric model based on the crystal structure. Based on the sequence, we classified the Pfam containing McpN-LBD and PilJ-LBD into three classes: sPilJ (single PilJ) represented by McpN-LBD with only one PilJ domain, dPilJ (dual PilJ) that contained dual PilJ domains, and hPilJ (hybrid PilJ) that comprises of a PilJ domain and another non-PilJ domain. Our work indicates a significant structural difference between the ligand binding domains of PilJ and McpN and will help our further study on both kinds of chemoreceptors. PubMed: 38484573DOI: 10.1016/j.bbrc.2024.149765 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.996 Å) |
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