8v7p | pdb_00008v7p

Crystal structure of the truncated P1 pilin from Pseudomonas aeruginosa

spinqualitylabelsall models 8v7p, resolution 1.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8v7p is a 1 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.3Å Ligands: CAD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FMK1_PSEAI Publication Abstract from PubMed The type IV pilus is a diverse molecular machine capable of conferring a variety of functions and is produced by a wide range of bacterial species. The ability of the pilus to perform host-cell adherence makes it a viable target for the development of vaccines against infection by human pathogens such as Pseudomonas aeruginosa. Here, the 1.3 A resolution crystal structure of the N-terminally truncated type IV pilin from P. aeruginosa strain P1 (DeltaP1) is reported, the first structure of its phylogenetically linked group (group I) to be discussed in the literature. The structure was solved from X-ray diffraction data that were collected 20 years ago with a molecular-replacement search model generated using AlphaFold; the effectiveness of other search models was analyzed. Examination of the high-resolution DeltaP1 structure revealed a solvent network that aids in maintaining the fold of the protein. On comparing the sequence and structure of P1 with a variety of type IV pilins, it was observed that there are cases of higher structural similarities between the phylogenetic groups of P. aeruginosa than there are between the same phylogenetic group, indicating that a structural grouping of pilins may be necessary in developing antivirulence drugs and vaccines. These analyses also identified the alpha-beta loop as the most structurally diverse domain of the pilins, which could allow it to serve a role in pilus recognition. Studies of DeltaP1 in vitro polymerization demonstrate that the optimal hydrophobic catalyst for the oligomerization of the pilus from strain K122 is not conducive for pilus formation of DeltaP1; a model of a three-start helical assembly using the DeltaP1 structure indicates that the alpha-beta loop and the D-loop prevent in vitro polymerization. The 1.3 A resolution structure of the truncated group Ia type IV pilin from Pseudomonas aeruginosa strain P1.,Bragagnolo N, Audette GF Acta Crystallogr D Struct Biol. 2024 Dec 1;80(Pt 12):834-849. doi: , 10.1107/S205979832401132X. Epub 2024 Nov 28. PMID:39607821 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA