5oiu

Crystal structure of PilF type IV pilus assembly ATPase from Thermus thermophilus

spinqualitylabelsall models 5oiu, resolution 2.44Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5oiu is a 6 chain structure with sequence from Thermus thermophilus HB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.44Å Ligands: ATP, CL, MG, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PILB_THET8 ATPase component of the type IV pilus (T4P) that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility facilitated by cycles of extension, adhesion, and retraction of T4P fibers (By similarity) (PubMed:29717025). Acts as a molecular motor to provide the energy that is required for biogenesis of the pilus and the extrusion of substrates generated in the cytoplasm (PubMed:27667690). PilB ATPase activity is also essential for T4P extension while antagonist PilT ATPase activity is required for T4P retraction (By similarity).[UniProtKB:P22608][UniProtKB:Q1D098] Publication Abstract from PubMed Type IV pili are responsible for a diverse range of functions, including twitching motility and cell adhesion. Assembly of the pilus fiber is driven by a cytoplasmic ATPase: it interacts with an inner membrane complex of biogenesis proteins which, in turn, bind to nascent pilin subunits and mediate fiber assembly. Here we report the structural characterization of the PilF TFP assembly ATPase from Thermus thermophilus. The crystal structure of a recombinant C-terminal fragment of PilF revealed bound, unhydrolysed ATP, although the full length complex was enzymatically active. 3D reconstructions were carried out by single particle cryoelectron microscopy for full length apoprotein PilF and in complex with AMPPNP. The structure forms an hourglass-like shape, with the ATPase domains in one half and the N1 domains in the second half which, we propose, interact with the other pilus biogenesis components. Molecular models for both forms were generated: binding of AMPPNP causes an upward shift of the N1 domains towards the ATPase domains of ~8 A. We advocate a model in which ATP hydrolysis is linked to displacement of the N1 domains which is associated with lifting pilin subunits out of the inner membrane, and provide the activation energy needed to form the pilus fiber. Structural cycle of the Thermus thermophilus PilF ATPase: the powering of type IVa pilus assembly.,Collins R, Karuppiah V, Siebert CA, Dajani R, Thistlethwaite A, Derrick JP Sci Rep. 2018 Sep 19;8(1):14022. doi: 10.1038/s41598-018-32218-3. PMID:30232337 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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