3R3K: Crystal Structure Of A Parallel 6-Helix Coiled Coil

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-A 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.
PDB ID: 3R3KDownload
MMDB ID: 95042
PDB Deposition Date: 2011/3/16
Updated in MMDB: 2011/12
Experimental Method:
x-ray diffraction
Resolution: 2.2  Å
Similar Structures:
Biological Unit for 3R3K: hexameric; determined by author and by software (PISA)
Molecular Components in 3R3K
Label Count Molecule
Proteins (6 molecules)
Cchex-phi22 Helix
Molecule annotation
Chemicals (16 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB