5w63

Crystal structure of channel catfish BAX

spinqualitylabelsall models 5w63, resolution 2.44Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5w63 is a 1 chain structure with sequence from Ictalurus punctatus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.436Å Ligands: EDO, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function E3TFZ1_ICTPU Publication Abstract from PubMed BAX and BAK are essential mediators of intrinsic apoptosis that permeabilize the mitochondrial outer membrane. BAX activation requires its translocation from cytosol to mitochondria where conformational changes cause its oligomerization. To better understand the critical step of translocation, we examined its blockade by mutation near the C terminus (P168G) or by antibody binding near the N terminus. Similarities in the crystal structures of wild-type and BAX P168G but significant other differences suggest that cytosolic BAX exists as an ensemble of conformers, and that the distribution of conformers within the ensemble determines the different functions of wild-type and mutant proteins. We also describe the structure of BAX in complex with an antibody, 3C10, that inhibits cytosolic BAX by limiting exposure of the membrane-associating helix alpha9, as does the P168G mutation. Our data for both means of BAX inhibition argue for an allosteric model of BAX regulation that derives from properties of the ensemble of conformers. Ensemble Properties of Bax Determine Its Function.,Robin AY, Iyer S, Birkinshaw RW, Sandow J, Wardak A, Luo CS, Shi M, Webb AI, Czabotar PE, Kluck RM, Colman PM Structure. 2018 Aug 4. pii: S0969-2126(18)30252-1. doi:, 10.1016/j.str.2018.07.006. PMID:30122452 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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