Crystal structures of the Chromobacterium violaceumω-transaminase reveal major structural rearrangements upon binding of coenzyme PLP.

@article{Humble2012CrystalSO,
  title={Crystal structures of the Chromobacterium violaceumω-transaminase reveal major structural rearrangements upon binding of coenzyme PLP.},
  author={Maria Svedendahl Humble and Karim Engelmark Cassimjee and Maria H{\aa}kansson and Yengo R Kimbung and Bj{\"o}rn Walse and Vahak Abedi and H -J. Federsel and Per Berglund and Derek T Logan},
  journal={The FEBS journal},
  year={2012},
  volume={279 5},
  pages={779-92}
}
UNLABELLED The bacterial ω-transaminase from Chromobacterium violaceum (Cv-ωTA, EC2.6.1.18) catalyses industrially important transamination reactions by use of the coenzyme pyridoxal 5'-phosphate (PLP). Here, we present four crystal structures of Cv-ωTA: two in the apo form, one in the holo form and one in an intermediate state, at resolutions between 1.35 and 2.4 Å. The enzyme is a homodimer with a molecular mass of ∼ 100 kDa. Each monomer has an active site at the dimeric interface that… CONTINUE READING