4IWB

Novel Fold of FliC/FliS Fusion Protein

Summary for 4IWB

• Entry DOI: 10.2210/pdb4iwb/pdb
• Related: 1ORY
• Descriptor: FliC, FliS chimera (2 entities in total)
• Functional Keywords: novel fold, motor protein
• Biological source: Aquifex aeolicus; More
• Total number of polymer chains: 2
• Total formula weight: 38584.56

Authors

Faham, S. (deposition date: 2013-01-23, release date: 2013-12-11, Last modification date: 2024-02-28)

Primary citation

Skorupka, K.,Han, S.K.,Nam, H.J.,Kim, S.,Faham, S.
Protein design by fusion: implications for protein structure prediction and evolution.
Acta Crystallogr.,Sect.D, 69:2451-2460, 2013

PubMed Abstract: Domain fusion is a useful tool in protein design. Here, the structure of a fusion of the heterodimeric flagella-assembly proteins FliS and FliC is reported. Although the ability of the fusion protein to maintain the structure of the heterodimer may be apparent, threading-based structural predictions do not properly fuse the heterodimer. Additional examples of naturally occurring heterodimers that are homologous to full-length proteins were identified. These examples highlight that the designed protein was engineered by the same tools as used in the natural evolution of proteins and that heterodimeric structures contain a wealth of information, currently unused, that can improve structural predictions.

PubMed: 24311586
DOI: 10.1107/S0907444913022701

Experimental method

X-RAY DIFFRACTION (1.75 Å)