5UVR
The core region of PilO from the type IV pilus system of Pseudomonas aeruginosa
Summary for 5UVR
| Entry DOI | 10.2210/pdb5uvr/pdb |
| Descriptor | PilO protein (2 entities in total) |
| Functional Keywords | alignment subcomplex, modified ferredoxin fold, reductive methylation, type iv pili, membrane protein |
| Biological source | Pseudomonas aeruginosa |
| Total number of polymer chains | 1 |
| Total formula weight | 10813.50 |
| Authors | Howell, P.L.,Junop, M.S. (deposition date: 2017-02-20, release date: 2018-02-21, Last modification date: 2023-10-04) |
| Primary citation | Leighton, T.L.,Mok, M.C.,Junop, M.S.,Howell, P.L.,Burrows, L.L. Conserved, unstructured regions in Pseudomonas aeruginosa PilO are important for type IVa pilus function. Sci Rep, 8:2600-2600, 2018 Cited by PubMed Abstract: Pseudomonas aeruginosa uses long, thin fibres called type IV pili (T4P) for adherence to surfaces, biofilm formation, and twitching motility. A conserved subcomplex of PilMNOP is required for extension and retraction of T4P. To better understand its function, we attempted to co-crystallize the soluble periplasmic portions of PilNOP, using reductive surface methylation to promote crystal formation. Only PilO crystallized; its structure was determined to 1.7 Å resolution using molecular replacement. This new structure revealed two novel features: a shorter N-terminal α1-helix followed by a longer unstructured loop, and a discontinuous β-strand in the second αββ motif, mirroring that in the first motif. PISA analysis identified a potential dimer interface with striking similarity to that of the PilO homolog EpsM from the Vibrio cholerae type II secretion system. We identified highly conserved residues within predicted unstructured regions in PilO proteins from various Pseudomonads and performed site-directed mutagenesis to assess their role in T4P function. R169D and I170A substitutions decreased surface piliation and twitching motility without disrupting PilO homodimer formation. These residues could form important protein-protein interactions with PilN or PilP. This work furthers our understanding of residues critical for T4aP function. PubMed: 29422606DOI: 10.1038/s41598-018-20925-w PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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