The Structural Basis of Coenzyme A Recycling in a Bacterial Organelle
Fig 4
Details of active site, dimeric assembly, and sequence conservation of PduL.
(a,b) Proposed active site of PduL with relevant residues shown as sticks in atom coloring (nitrogen blue, oxygen red, sulfur yellow), zinc as grey colored spheres and coordinating ordered water molecules in red. Distances between atom centers are indicated in Å. (a) Coenzyme A containing, (b) phosphate-bound structure. (c) View of the dimer in the asymmetric unit from the side, domains 1 and 2 colored as in Fig 2 and the two chains differentiated by blue/red versus slate/firebrick. The bottom panel shows a top view down the 2-fold axis as indicated by the arrow in the top panel. The asterisk and double arrow marks the location of the π–π interaction between F116 and the CoA base of the other dimer chain. (d) Surface representation of the structure with indicated conservation (red: high, white: intermediate, yellow: low).