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1.
Angew Chem Int Ed Engl ; 53(3): 824-8, 2014 Jan 13.
Article in English | MEDLINE | ID: mdl-24302672

ABSTRACT

Echinomycin is a nonribosomal depsipeptide natural product with a range of interesting bioactivities that make it an important target for drug discovery and development. It contains a thioacetal bridge, a unique chemical motif derived from the disulfide bond of its precursor antibiotic triostin A by the action of an S-adenosyl-L-methionine-dependent methyltransferase, Ecm18. The crystal structure of Ecm18 in complex with its reaction products S-adenosyl-L-homocysteine and echinomycin was determined at 1.50 Å resolution. Phasing was achieved using a new molecular replacement package called AMPLE, which automatically derives search models from structure predictions based on ab initio protein modelling. Structural analysis indicates that a combination of proximity effects, medium effects, and catalysis by strain drives the unique transformation of the disulfide bond into the thioacetal linkage.


Subject(s)
Disulfides/chemistry , Echinomycin/biosynthesis , Catalysis , Crystallography, X-Ray , Echinomycin/chemistry , Homocysteine/biosynthesis , Homocysteine/chemistry , Hydrogen Bonding , Methionine/chemistry , Methionine/metabolism , Methyltransferases/metabolism , Protein Structure, Tertiary , Quinoxalines/chemistry
2.
Extremophiles ; 11(3): 463-7, 2007 May.
Article in English | MEDLINE | ID: mdl-17225927

ABSTRACT

The Pacific nodule province covered about 4.5 million km(2) in the east tropical Pacific with an abundance of polymetallic nodules at the seafloor. In view of the environmental protection and resource preservation, the survey of biodiversity was important during the reconnaissance and exploitation in this area. As one of the important component of the deep sea ecosystem, the microbial community in the Pacific nodule province was still largely unknown. The chitinolytic bacteria diversity in deep-sea sediment of a station within the Pacific nodule province was examined by molecular technology. A total of 18 chitinase genes were detected by a set of degenerate PCR primer specific for chiA gene fragment of family 18 chitinase. Most of them belonged to the Serratia-like chitinase. Eight genes had different amino acid sequences in the conserved motif, encompassing the catalytic site among the ChiA protein of family 18 glycosyl hydrolases, and clustered in an independent clade on the phylygenetic tree.


Subject(s)
Bacteria/genetics , Chitinases/genetics , Amino Acid Sequence , Bacteria/classification , Base Sequence , Chitinases/chemistry , DNA Primers , Molecular Sequence Data , Phylogeny , Sequence Homology, Amino Acid , Water Microbiology
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