8BCS

X-ray crystal structure of a de novo designed helix-loop-helix homodimer in an anti arrangement, CC-HP1.0

8BCS の概要

• エントリーDOI: 10.2210/pdb8bcs/pdb
• 分子名称: CC-HP1.0, ACETATE ION (2 entities in total)
• 機能のキーワード: coiled coil, 4-helix bundle, de novo protein design, helix-loop-helix dimer, de novo protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5334.31

構造登録者

Edgell, C.L.,Mylemans, B.,Naudin, E.A.,Smith, A.J.,Savery, N.J.,Woolfson, D.N. (登録日: 2022-10-17, 公開日: 2023-06-07, 最終更新日: 2024-10-16)

主引用文献

Smith, A.J.,Naudin, E.A.,Edgell, C.L.,Baker, E.G.,Mylemans, B.,FitzPatrick, L.,Herman, A.,Rice, H.M.,Andrews, D.M.,Tigue, N.,Woolfson, D.N.,Savery, N.J.
Design and Selection of Heterodimerizing Helical Hairpins for Synthetic Biology.
Acs Synth Biol, 12:1845-1858, 2023

PubMed Abstract: Synthetic biology applications would benefit from protein modules of reduced complexity that function orthogonally to cellular components. As many subcellular processes depend on peptide-protein or protein-protein interactions, designed polypeptides that can bring together other proteins controllably are particularly useful. Thanks to established sequence-to-structure relationships, helical bundles provide good starting points for such designs. Typically, however, such designs are tested and function in cells is not guaranteed. Here, we describe the design, characterization, and application of helical hairpins that heterodimerize to form 4-helix bundles in cells. Starting from a rationally designed homodimer, we construct a library of helical hairpins and identify complementary pairs using bimolecular fluorescence complementation in . We characterize some of the pairs using biophysics and X-ray crystallography to confirm heterodimeric 4-helix bundles. Finally, we demonstrate the function of an exemplar pair in regulating transcription in both and mammalian cells.

PubMed: 37224449
DOI: 10.1021/acssynbio.3c00231

実験手法

X-RAY DIFFRACTION (2.1 Å)