Fig. 7: Comparison of AdoCbl binding and light induced changes in photocobilin and CarH proteins.
From: Photocobilins integrate B12 and bilin photochemistry for enzyme control

AdoCbl binding in TtCarH (a), AbPcob (b) and SasPcob (c) are shown as line and sticks. AdoCbl molecules are shown as magenta and upper ligands as cyan. Residues involved with binding are shown as blue and green sticks. The residues in the opposite monomer are shown as grey. Overall structural changes in TtCarH (d) and SasPcob (e). The protein is shown as a cartoon. The main monomer in dark state as blue and light state as cyan. The opposite monomer as grey. The AdoCbl molecules are shown as sticks with dark state as blue and light state as cyan. Upper adenosyl group is shown as red stick. BV molecules in SasPCob are shown as grey spheres. Main residues involved in the change are shown as blue and cyan sticks for dark and light state. The arrow indicates the direction in which the protein moves, while the length of the arrow represents the scale of the movement. The circular perspective provides a more detailed observation of the dynamic motion of residues within dark and light structure. Residues in the opposite monomer are displayed as grey sticks and red dots. f Representation of photochemical changes in Pcob protein. The AdoCbl and BV molecules are shown as pink and yellow sticks, adenosyl as cyan sticks. Red, green and blue blocks represent for four helix bundle, Rossmann fold and BV binding regions in the Pcob protein.