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3R3K

Crystal structure of a parallel 6-helix coiled coil

Summary for 3R3K
Entry DOI10.2210/pdb3r3k/pdb
Related3R46 3R47 3R48
DescriptorCChex-Phi22 helix, CHLORIDE ION, SODIUM ION, ... (5 entities in total)
Functional Keywordsparallel hexamer, kih interactions, hydrophobic channel, synthetic biology, de novo protein
Total number of polymer chains3
Total formula weight10720.68
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 citationZaccai, 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: 22037471
DOI: 10.1038/nchembio.692
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2009 Å)
Structure validation

237735

数据于2025-06-18公开中

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