Ontology highlight
ABSTRACT:
SUBMITTER: Bera AK
PROVIDER: S-EPMC2879354 | biostudies-literature | 2010 Jun
REPOSITORIES: biostudies-literature
Bera Asim K AK Atanasova Vesna V Gamage Swarna S Robinson Howard H Parsons James F JF
Acta crystallographica. Section D, Biological crystallography 20100515 Pt 6
The structure of EhpF, a 41 kDa protein that functions in the biosynthetic pathway leading to the broad-spectrum antimicrobial compound D-alanylgriseoluteic acid (AGA), is reported. A cluster of approximately 16 genes, including ehpF, located on a 200 kbp plasmid native to certain strains of Pantoea agglomerans encodes the proteins that are required for the conversion of chorismic acid to AGA. Phenazine-1,6-dicarboxylate has been identified as an intermediate in AGA biosynthesis and deletion of ...[more]