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-Structure paper
タイトル | Cryoelectron-Microscopic Structure of the pKpQIL Conjugative Pili from Carbapenem-Resistant Klebsiella pneumoniae. |
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ジャーナル・号・ページ | Structure, Vol. 28, Issue 12, Page 1321-11328.e2, Year 2020 |
掲載日 | 2020年12月1日 |
著者 | Weili Zheng / Alejandro Pena / Wen Wen Low / Joshua L C Wong / Gad Frankel / Edward H Egelman / |
PubMed 要旨 | Conjugative pili are important in mediating bacterial conjugation and horizontal gene transfer. Since plasmid transfer can include antibiotic-resistance genes, conjugation is an important mechanism ...Conjugative pili are important in mediating bacterial conjugation and horizontal gene transfer. Since plasmid transfer can include antibiotic-resistance genes, conjugation is an important mechanism in the spread of antibiotic resistance. Filamentous bacteriophages have been shown to exist in two different structural classes: those with a 5-fold rotational symmetry and those with a one-start helix with approximately 5 subunits per turn. Structures for the F and the F-like pED208 conjugation pilus have shown that they have 5-fold rotational symmetry. Here, we report the cryoelectron-microscopic structure of conjugative pili from carbapenem-resistant Klebsiella pneumoniae, encoded on the IncFIIK pKpQIL plasmid, at 3.9 Å resolution and show that it has a one-start helix. These results establish that conjugation pili can exist in at least two structural classes, consistent with other results showing that relatively small perturbations are needed to change the helical symmetry of polymers. |
リンク | Structure / PubMed:32916103 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 3.9 Å |
構造データ | EMDB-22460, PDB-7jsv: |
化合物 | ChemComp-LHG: |
由来 |
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キーワード | PROTEIN FIBRIL / Conjugation pili / Helical reconstruction |