Journal
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume 60, Issue 4, Pages 778-786Publisher
WILEY
DOI: 10.1002/prot.20548
Keywords
PhzF family; gene duplication and fusion; domain swapping
Categories
Ask authors/readers for more resources
In the Pseudomonas bacterial genomes, the PhzF proteins are involved in the production of phenazine derivative antibiotic and antifungal compounds. The PhzF superfamily however also encompasses proteins in all genomes from bacteria to eukaryotes, for which no function has been assigned. We have determined the three dimensional crystal structure at 2.05 angstrom resolution of YHI9, the yeast member of the PhzF family. YHI9 has a fold similar to bacterial diaminopimelate epimerase, revealing a bimodular structure with an internal symmetry. Residue conservation identifies a putative active site at the interface between the two domains. Evolution of this protein by gene duplication, gene fusion and domain swapping from an ancestral gene containing the hot dog fold, identifies the protein as a kinked double hot dog fold.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available