4ZSX

Structure of a fusion protein with a helix linker, 2ARH-3-3KAW-2.0

Summary for 4ZSX

• Entry DOI: 10.2210/pdb4zsx/pdb
• Related: 4ZSV 4ZSZ
• Descriptor: Uncharacterized Fusion Protein, PHOSPHATE ION (3 entities in total)
• Functional Keywords: protein design, bionanotechnology, protein assembly, symmetry, biomaterials, unknown function
• Biological source: Aquifex aeolicus; More
• Total number of polymer chains: 2
• Total formula weight: 68772.27

Authors

Lai, Y.-T.,Yeates, T.O. (deposition date: 2015-05-14, release date: 2015-08-19, Last modification date: 2023-09-27)

Primary citation

Lai, Y.T.,Jiang, L.,Chen, W.,Yeates, T.O.
On the predictability of the orientation of protein domains joined by a spanning alpha-helical linker.
Protein Eng.Des.Sel., 28:491-500, 2015

PubMed Abstract: 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°. 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.

PubMed: 26243886
DOI: 10.1093/protein/gzv035

Experimental method

X-RAY DIFFRACTION (2.19 Å)