6VE3
Tetradecameric PilQ from Pseudomonas aeruginosa
Summary for 6VE3
| Entry DOI | 10.2210/pdb6ve3/pdb |
| EMDB information | 21152 21153 21154 |
| Descriptor | Fimbrial assembly protein PilQ (1 entity in total) |
| Functional Keywords | type iv pilus, t4p, pilq, secretin, type iva pilus, t4ap, pilus, outer membrane, periplasm, bacterial secretion system, protein transport |
| Biological source | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Total number of polymer chains | 14 |
| Total formula weight | 1116235.97 |
| Authors | McCallum, M.,Tammam, S.,Rubinstein, J.L.,Burrows, L.L.,Howell, P.L. (deposition date: 2019-12-28, release date: 2020-12-23, Last modification date: 2024-03-06) |
| Primary citation | McCallum, M.,Tammam, S.,Rubinstein, J.L.,Burrows, L.L.,Howell, P.L. CryoEM map of Pseudomonas aeruginosa PilQ enables structural characterization of TsaP. Structure, 29:457-, 2021 Cited by PubMed Abstract: The type IV pilus machinery is a multi-protein complex that polymerizes and depolymerizes a pilus fiber used for attachment, twitching motility, phage adsorption, natural competence, protein secretion, and surface-sensing. An outer membrane secretin pore is required for passage of the pilus fiber out of the cell. Herein, the structure of the tetradecameric secretin, PilQ, from the Pseudomonas aeruginosa type IVa pilus system was determined to 4.3 Å and 4.4 Å resolution in the presence and absence of C symmetric spikes, respectively. The heptameric spikes were found to be two tandem C-terminal domains of TsaP. TsaP forms a belt around PilQ and while it is not essential for twitching motility, overexpression of TsaP triggers a signal cascade upstream of PilY1 leading to cyclic di-GMP up-regulation. These results resolve the identity of the spikes identified with Proteobacterial PilQ homologs and may reveal a new component of the surface-sensing cyclic di-GMP signal cascade. PubMed: 33338410DOI: 10.1016/j.str.2020.11.019 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.3 Å) |
Structure validation
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