Structures of the Ca2+-regulated photoprotein obelin Y138F mutant before and after bioluminescence support the catalytic function of a water molecule in the reaction

Natashin, P.V.; Ding, W.; Eremeeva, E.V.; Markova, S.V.; Lee, J.; Vysotski, E.S.; Liu, Z.-J.

doi:10.1107/S1399004713032434

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 4
Internal cavities of Ca²⁺-discharged WT and Y138F obelins. (a) Two-dimensional drawing of the hydrogen-bonding network in the binding cavities of Ca²⁺-discharged WT (left panel) and Y138F (right panel) obelins. (b) Stereoview of the superposition of coelenteramide molecules with the key residues facing into the internal cavities of Ca²⁺-discharged WT (brown) and Y138F (blue) obelins. Hydrogen bonds are shown as dashed lines. Distances are given in Å. Water molecules are shown as balls coloured according to the structure. (c) Electron-density maps of 2-hydroperoxycoelenterazine (left) and coelenteramide (right) molecules with some internal cavity residues in Y138F obelin before (state II) and after (state III) the bioluminescence reaction, respectively.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 70| Part 3| February 2014| Pages 720-732

doi:10.1107/S1399004713032434

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