8u2b

Cryo-EM structure of C.crescentus bNY30a pilus complexCryo-EM structure of C.crescentus bNY30a pilus complex

Structural highlights 8u2b is a 37 chain structure with sequence from Caulobacter vibrioides. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.8Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A290MFS9_CAUVI Publication Abstract from PubMed Caulobacter crescentus Tad (tight adherence) pili, part of the type IV pili family, are crucial for mechanosensing, surface adherence, bacteriophage (phage) adsorption, and cell-cycle regulation. Unlike other type IV pilins, Tad pilins lack the typical globular beta sheet domain responsible for pilus assembly and phage binding. The mechanisms of Tad pilus assembly and its interaction with phage PhiCb5 have been elusive. Using cryo-electron microscopy, we unveiled the Tad pilus assembly mechanism, featuring a unique network of hydrogen bonds at its core. We then identified the Tad pilus binding to the PhiCb5 maturation protein (Mat) through its beta region. Notably, the amino terminus of PhiCb5 Mat is exposed outside the capsid and phage/pilus interface, enabling the attachment of fluorescent and affinity tags. These engineered PhiCb5 virions can be efficiently assembled and purified in Escherichia coli, maintaining infectivity against C. crescentus, which presents promising applications, including RNA delivery and phage display. Structural mechanisms of Tad pilus assembly and its interaction with an RNA virus.,Wang Y, Theodore M, Xing Z, Narsaria U, Yu Z, Zeng L, Zhang J Sci Adv. 2024 May 3;10(18):eadl4450. doi: 10.1126/sciadv.adl4450. Epub 2024 May , 3. PMID:38701202 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 8u2b, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image