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Figure 1
Comparison of similar active sites. (a) Synechocystis sp. PCC 6803 structure (PDB entry 3rpl , yellow) shown with key active-site residues shown as sticks (Asp33, Glu57, Glu100, Thr102, Tyr131, Lys134, Arg176, Arg178, Asp198, Asp200 and Glu225). (b) T. elongatus structure (PDB entry 5a5l , purple) bound with sedoheptulose-7-phosphate (lavender) with equivalent active-site residues shown as sticks (Asp33, Glu57, Glu100, Thr102, Tyr131, Lys134, Arg176, Arg178, Asp198, Asp200 and Glu225). Magnesium ions are shown as spheres. The phosphate (PO4) of the suggested product complex is clearly visible. Ligand OMIT map difference density is shown for the S7P ligand and phosphate (lavender mesh) using a 4σ contour level. Active-site residues and metals are in the same conformation; selectivity between the sugars is not the result of large-scale conformational change.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 71| Part 10| October 2015| Pages 1341-1345
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