3R3K
Crystal structure of a parallel 6-helix coiled coil
Summary for 3R3K
Entry DOI | 10.2210/pdb3r3k/pdb |
Related | 3R46 3R47 3R48 |
Descriptor | CChex-Phi22 helix, CHLORIDE ION, SODIUM ION, ... (5 entities in total) |
Functional Keywords | parallel hexamer, kih interactions, hydrophobic channel, synthetic biology, de novo protein |
Total number of polymer chains | 3 |
Total formula weight | 10720.68 |
Authors | Zaccai, N.R.,Chi, B.H.C.,Woolfson, D.N.,Brady, R.L. (deposition date: 2011-03-16, release date: 2011-11-16, Last modification date: 2025-03-26) |
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 Cited by 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: 22037471DOI: 10.1038/nchembio.692 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2009 Å) |
Structure validation
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