5ft1 | pdb_00005ft1

Crystal structure of gp37(Dip) from bacteriophage phiKZ bound to RNase E of Pseudomonas aeruginosa

spinqualitylabelsall models 5ft1, resolution 2.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ft1 is a 12 chain structure with sequence from Pseudomonas aeruginosa and Pseudomonas virus phiKZ. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.75Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8SDC5_BPDPK Publication Abstract from PubMed In all domains of life, the catalysed degradation of RNA facilitates rapid adaptation to changing environmental conditions, while destruction of foreign RNA is an important mechanism to prevent host infection. We have identified a virus-encoded protein termed gp37/Dip, which directly binds and inhibits the RNA degradation machinery of its bacterial host. Encoded by giant phage PhiKZ, this protein associates with two RNA binding sites of the RNase E component of the Pseudomonas aeruginosa RNA degradosome, occluding them from substrates and resulting in effective inhibition of RNA degradation and processing. The 2.2 A crystal structure reveals that this novel homo-dimeric protein has no identifiable structural homologues. Our biochemical data indicate that acidic patches on the convex outer surface bind RNase E. Through the activity of Dip, PhiKZ has evolved a unique mechanism to down regulate a key metabolic process of its host to allow accumulation of viral RNA in infected cells. Structural elucidation of a novel mechanism for the bacteriophage-based inhibition of the RNA degradosome.,Van den Bossche A, Hardwick SW, Ceyssens PJ, Hendrix H, Voet M, Dendooven T, Bandyra KJ, De Maeyer M, Aertsen A, Noben JP, Luisi BF, Lavigne R Elife. 2016 Jul 22;5. pii: e16413. doi: 10.7554/eLife.16413. PMID:27447594 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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