1YM5

Crystal structure of YHI9, the yeast member of the phenazine biosynthesis PhzF enzyme superfamily.

Summary for 1YM5

• Entry DOI: 10.2210/pdb1ym5/pdb
• Descriptor: Hypothetical 32.6 kDa protein in DAP2-SLT2 intergenic region (2 entities in total)
• Functional Keywords: phzf enzyme superfamily, double hot-dog, structural genomics, paris-sud yeast structural genomics, ysg, oxidoreductase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 1
• Total formula weight: 33427.24

Authors

Liger, D.,Quevillon-Cheruel, S.,Sorel, I.,Bremang, M.,Blondeau, K.,Aboulfath, I.,Janin, J.,Van Tilbeurgh, H.,Leulliot, N.,Paris-Sud Yeast Structural Genomics (YSG) (deposition date: 2005-01-20, release date: 2005-08-02, Last modification date: 2024-03-13)

Primary citation

Liger, D.,Quevillon-Cheruel, S.,Sorel, I.,Bremang, M.,Blondeau, K.,Aboulfath, I.,Janin, J.,van Tilbeurgh, H.,Leulliot, N.
Crystal structure of YHI9, the yeast member of the phenazine biosynthesis PhzF enzyme superfamily
Proteins, 60:778-786, 2005

PubMed Abstract: 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 A 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.

PubMed: 16021630
DOI: 10.1002/prot.20548

Experimental method

X-RAY DIFFRACTION (2.05 Å)