6a9s

The crystal structure of vaccinia virus A26 (residues 1-397)

spinqualitylabelsall models 6a9s, resolution 1.18Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6a9s is a 1 chain structure with sequence from Vaccinia virus WR. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.18Å Ligands: EDO, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PG153_VACCW Envelop protein that mediates acid-dependent endocytosis into host cells (PubMed:20538855). Plays an important role in endocytic entry of the virus by acting as an acid-sensitive membrane fusion suppressor (PubMed:22278246, PubMed:31220181). Low pH in host endosomes triggers conformational changes to allow de-repression of viral fusion complex activity and membrane fusion within vesicles (PubMed:31220181). Plays also a role in bridging the mature virion with structural protein OPG152. Publication Abstract from PubMed Vaccinia mature virus requires A26 envelope protein to mediate acid-dependent endocytosis into HeLa cells in which we hypothesized that A26 protein functions as an acid-sensitive membrane fusion suppressor. Here, we provide evidence showing that N-terminal domain (aa1-75) of A26 protein is an acid-sensitive region that regulates membrane fusion. Crystal structure of A26 protein revealed that His48 and His53 are in close contact with Lys47, Arg57, His314 and Arg312, suggesting that at low pH these His-cation pairs could initiate conformational changes through protonation of His48 and His53 and subsequent electrostatic repulsion. All the A26 mutant mature viruses that interrupted His-cation pair interactions of His48 and His 53 indeed have lost virion infectivity. Isolation of revertant viruses revealed that second site mutations caused frame shifts and premature termination of A26 protein such that reverent viruses regained cell entry through plasma membrane fusion. Together, we conclude that viral A26 protein functions as an acid-sensitive fusion suppressor during vaccinia mature virus endocytosis. Vaccinia viral A26 protein is a fusion suppressor of mature virus and triggers membrane fusion through conformational change at low pH.,Chang HW, Yang CH, Luo YC, Su BG, Cheng HY, Tung SY, Carillo KJD, Liao YT, Tzou DM, Wang HC, Chang W PLoS Pathog. 2019 Jun 20;15(6):e1007826. doi: 10.1371/journal.ppat.1007826., eCollection 2019 Jun. PMID:31220181 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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