4ZSZ: Structure of a fusion protein with a helix linker, 2ARH-3-3KAW-3.0

Connecting proteins together in prescribed geometric arrangements is an important element in new areas of biomolecular design. In this study, we characterize the degree of three-dimensional orientational control that can be achieved when two protein domains that have alpha-helical termini are joined using an alpha-helical linker. A fusion between naturally oligomeric protein domains was designed in this fashion with the intent of creating a self-assembling 12-subunit tetrahedral protein cage. While the designed fusion protein failed to assemble into a tetrahedral cage in high yield, a series of crystal structures showed that the two fused components were indeed bridged by an intact alpha helix, although the fusion protein was distorted from the intended ideal configuration by bending of the helix, ranging from 7 to 35 degrees . That range of deviation in orientation creates challenges for designing large, perfectly symmetric protein assemblies, although it should offer useful outcomes for other less geometrically demanding applications in synthetic biology.
PDB ID: 4ZSZDownload
MMDB ID: 131938
PDB Deposition Date: 2015/5/14
Updated in MMDB: 2017/12
Experimental Method:
x-ray diffraction
Resolution: 4.251  Å
Source Organism:
Similar Structures:
Biological Unit for 4ZSZ: tetrameric; determined by author and by software (PISA)
Molecular Components in 4ZSZ
Label Count Molecule
Proteins (4 molecules)
Uncharacterized Fusion Protein
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB