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Title | CryoEM map of Pseudomonas aeruginosa PilQ enables structural characterization of TsaP. |
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Journal, issue, pages | Structure, Vol. 29, Issue 5, Page 457-466.e4, Year 2021 |
Publish date | May 6, 2021 |
Authors | Matthew McCallum / Stephanie Tammam / John L Rubinstein / Lori L Burrows / P Lynne Howell / |
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 ...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. |
External links | Structure / PubMed:33338410 |
Methods | EM (single particle) |
Resolution | 4.3 - 6.9 Å |
Structure data | EMDB-21152, PDB-6ve2: EMDB-21153, PDB-6ve3: EMDB-21154, PDB-6ve4: |
Source |
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Keywords | PROTEIN TRANSPORT / Type IV pilus / T4P / PilQ / TsaP / secretin / pilotin / type IVa pilus / T4aP / pilus / outer membrane / periplasm / bacterial secretion system |