5ehb

A de novo designed hexameric coiled-coil peptide with iodotyrosine

spinqualitylabelsall models 5ehb, resolution 3.19Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ehb is a 2 chain structure with sequence from Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.19Å Ligands: IYR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Protein conformational switches have many useful applications but are difficult to design rationally. Here we demonstrate how the isoenergetic energy landscape of higher-order coiled coils can enable the formation of an oligomerization switch by insertion of a single destabilizing element into an otherwise stable computationally designed scaffold. We describe a de novo designed peptide that was discovered to switch between a parallel symmetric pentamer at pH 8 and a trimer of antiparallel dimers at pH 6. The transition between pentamer and hexamer is caused by changes in the protonation states of glutamatic acid residues with highly upshifted pKa values in both oligomer forms. The drastic conformational change coupled with the narrow pH range makes the peptide sequence an attractive candidate for introduction of pH sensing into other proteins. The results highlight the remarkable ability of simple-alpha helices to self-assemble into a vast range of structural states. A De Novo Designed Coiled-Coil Peptide with a Reversible pH-Induced Oligomerization Switch.,Lizatovic R, Aurelius O, Stenstrom O, Drakenberg T, Akke M, Logan DT, Andre I Structure. 2016 Jun 7;24(6):946-55. doi: 10.1016/j.str.2016.03.027. Epub 2016 May, 5. PMID:27161978 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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