Crystal Structure of the R253A Mutant of 7,8-Diaminopelargonic Acid Synthase

Conserved and nonconserved residues in the substrate binding site of 7,8-diaminopelargonic acid synthase from Escherichia coli are essential for catalysis.

Adenosylmethionine-8-amino-7-oxononanoate aminotransferase

7,8-diamino-pelargonic acid aminotransferase, DAPA aminotransferase

PEG4000, MPD, HEPES, isopropanol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K

WT structure of 7,8-Diaminopelargonic Acid Synthase

7,8-Diaminopelargonic Acid Synthase in Complex with the KAPA Substrate

7,8-Diaminopelargonic Acid Synthase in Complex with cis-Amiclenomycin

7,8-Diaminopelargonic Acid Synthase in Complex with trans-Amiclenomycin

R391A mutant of 7,8-Diaminopelargonic Acid Synthase

Crystal Structure of the R253K Mutant of 7,8-Diaminopelargonic Acid Synthase

Crystal Structure of the D147N Mutant of 7,8-Diaminopelargonic Acid Synthase

Crystal Structure of the Y144F Mutant of 7,8-Diaminopelargonic Acid Synthase

Crystal Structure of the Y17F Mutant of 7,8-Diaminopelargonic Acid Synthase

The crystallised protein differs from the Swissprot sequence at residue 14. In the Swissprot sequence number 14 is a tryptophan while in this structure it is a leucin. This is confirmed by DNA sequencing and was also reported for the original wild-type structure (1qj5).

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

Aminotransferase, Fold type I, subclass II, homodimer, TRANSFERASE