3hx6

Crystal structure of Pseudomonas aeruginosa PilY1 C-terminal domain

spinqualitylabelsall models 3hx6, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3hx6 is a 2 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 2.1Å Ligands: CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PILY1_PSEAE Involved in pilus assembly, twitching motility and adhesion to host cells. Primes type IV pili (T4P) assembly and is required for inclusion of minor pilins PilV, PilW and PilX to the surface pili (PubMed:25389296). Stabilizes assembled pilus fibers likely by antagonizing retraction mediated by PilT. Calcium-binding and calcium release by PilY1 seem to be essential for twitching motility and for regulation of pilus retraction dynamics of PilT (By similarity).[UniProtKB:S0HPF7] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Several bacterial pathogens require the "twitching" motility produced by filamentous type IV pili (T4P) to establish and maintain human infections. Two cytoplasmic ATPases function as an oscillatory motor that powers twitching motility via cycles of pilus extension and retraction. The regulation of this motor, however, has remained a mystery. We present the 2.1 A resolution crystal structure of the Pseudomonas aeruginosa pilus-biogenesis factor PilY1, and identify a single site on this protein required for bacterial translocation. The structure reveals a modified beta-propeller fold and a distinct EF-hand-like calcium-binding site conserved in pathogens with retractile T4P. We show that preventing calcium binding by PilY1 using either an exogenous calcium chelator or mutation of a single residue disrupts Pseudomonas twitching motility by eliminating surface pili. In contrast, placing a lysine in this site to mimic the charge of a bound calcium interferes with motility in the opposite manner-by producing an abundance of nonfunctional surface pili. Our data indicate that calcium binding and release by the unique loop identified in the PilY1 crystal structure controls the opposing forces of pilus extension and retraction. Thus, PilY1 is an essential, calcium-dependent regulator of bacterial twitching motility. Crystal structure analysis reveals Pseudomonas PilY1 as an essential calcium-dependent regulator of bacterial surface motility.,Orans J, Johnson MD, Coggan KA, Sperlazza JR, Heiniger RW, Wolfgang MC, Redinbo MR Proc Natl Acad Sci U S A. 2009 Dec 28. PMID:20080557 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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