6IKI
Crystal structure of YfiB(W55L)
Summary for 6IKI
| Entry DOI | 10.2210/pdb6iki/pdb |
| Descriptor | YfiB, GLYCEROL, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | signalling system; peptidoglycan binding, signaling protein |
| Biological source | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Total number of polymer chains | 2 |
| Total formula weight | 36910.03 |
| Authors | Li, S.,Zhang, Q.,Bartlam, M. (deposition date: 2018-10-16, release date: 2019-03-13, Last modification date: 2023-11-22) |
| Primary citation | Li, S.,Li, T.,Teng, X.,Lou, X.,Xu, Y.,Zhang, Q.,Bartlam, M. Structural analysis of activating mutants of YfiB from Pseudomonas aeruginosa PAO1. Biochem. Biophys. Res. Commun., 506:997-1003, 2018 Cited by PubMed Abstract: Bacterial cyclic-di-GMP (c-di-GMP) is an important messenger molecule that influences diverse cellular processes including motility, virulence and cytotoxicity systems, polysaccharide synthesis and biofilm formation. The YfiBNR tripartite signalling system in P. aeruginosa modulates the cellular c-di-GMP levels in response to signals received from the periplasm. In this study, we analyse the structures of activating mutants of the outer membrane protein YfiB that give rise to increased surface attachment and biofilm formation. The F48S and W55L mutants of YfiB(27-168) crystallize in the same dimeric arrangement as our previously reported YfiB structures that preclude complex formation with YfiR. The L43P mutant of YfiB(27-168) is monomeric and forms a stable complex with YfiR. The YfiB(L43P)-YfiR crystal structure reveals a dramatic rearrangement of the N-terminal fragment, which is implicated in increased YfiB activation and membrane attachment, upon YfiR binding. Comparison with our previous complex structure between YfiB(59-168) and YfiR reveals extensive interactions between the N-terminal fragment of YfiB (residues 35-55) and YfiR. PubMed: 30404734DOI: 10.1016/j.bbrc.2018.10.190 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.204 Å) |
Structure validation
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