3R47

Crystal structure of a 6-helix coiled coil CC-hex-H24

Summary for 3R47

• Entry DOI: 10.2210/pdb3r47/pdb
• Related: 3R3K 3R46 3R48
• Descriptor: coiled coil helix L24H, BROMIDE ION (3 entities in total)
• Functional Keywords: coiled coil domain, hexamer, kih interactions, hydrophobic channel, synthetic biology, de novo protein
• Biological source: Synthetic construct
• Total number of polymer chains: 12
• Total formula weight: 40815.69

Authors

Zaccai, N.R.,Chi, B.H.C.,Woolfson, D.N.,Brady, R.L. (deposition date: 2011-03-17, release date: 2011-11-16, Last modification date: 2023-09-13)

Primary citation

Zaccai, N.R.,Chi, B.,Thomson, A.R.,Boyle, A.L.,Bartlett, G.J.,Bruning, M.,Linden, N.,Sessions, R.B.,Booth, P.J.,Brady, R.L.,Woolfson, D.N.
A de novo peptide hexamer with a mutable channel.
Nat.Chem.Biol., 7:935-941, 2011

PubMed Abstract: The design of new proteins that expand the repertoire of natural protein structures represents a formidable challenge. Success in this area would increase understanding of protein structure and present new scaffolds that could be exploited in biotechnology and synthetic biology. Here we describe the design, characterization and X-ray crystal structure of a new coiled-coil protein. The de novo sequence forms a stand-alone, parallel, six-helix bundle with a channel running through it. Although lined exclusively by hydrophobic leucine and isoleucine side chains, the 6-Å channel is permeable to water. One layer of leucine residues within the channel is mutable, accepting polar aspartic acid and histidine side chains, which leads to subdivision and organization of solvent within the lumen. Moreover, these mutants can be combined to form a stable and unique (Asp-His)(3) heterohexamer. These new structures provide a basis for engineering de novo proteins with new functions.

PubMed: 22037471
DOI: 10.1038/nchembio.692

Experimental method

X-RAY DIFFRACTION (2.5002 Å)