6rvu

Crystal structure of the Burkholderia Lethal Factor 1 (BLF1)

spinqualitylabelsall models 6rvu, resolution 0.99Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6rvu is a 1 chain structure with sequence from Burkholderia pseudomallei K96243. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 0.99Å Ligands: EDO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q63UP7_BURPS Publication Abstract from PubMed Burkholderia pseudomallei lethal factor 1 (BLF1) exhibits site-specific glutamine deamidase activity against the eukaryotic RNA helicase, eIF4A, thereby blocking mammalian protein synthesis. The structure of a complex between BLF1 C94S and human eIF4A shows that the toxin binds in the cleft between the two RecA-like eIF4A domains forming interactions with residues from both and with the scissile amide of the target glutamine, Gln339, adjacent to the toxin active site. The RecA-like domains adopt a radically twisted orientation compared to other eIF4A structures and the nature and position of conserved residues suggests this may represent a conformation associated with RNA binding. Comparison of the catalytic site of BLF1 with other deamidases and cysteine proteases reveals that they fall into two classes, related by pseudosymmetry, that present either the re or si faces of the target amide/peptide to the nucleophilic sulfur, highlighting constraints in the convergent evolution of their Cys-His active sites. Molecular basis of specificity and deamidation of eIF4A by Burkholderia Lethal Factor 1.,Mobbs GW, Aziz AA, Dix SR, Blackburn GM, Sedelnikova SE, Minshull TC, Dickman MJ, Baker PJ, Nathan S, Raih MF, Rice DW Commun Biol. 2022 Mar 28;5(1):272. doi: 10.1038/s42003-022-03186-2. PMID:35347220 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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