Crystal Structure of the Unliganded Alkaline Protease from Pseudomonas aeruginosa IFO3080 and Its Conformational Changes on Ligand Binding1

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Abstract
The crystal structure of the unliganded alkaline protease from Pseudomonas aeruginosa IF03080 has been determined at 2.0 A resolution by the X-ray method. The enzyme consists of N-terminal catalytic and C-terminal β-helix domains. On structural comparison between the present unliganded enzyme and structurally-known liganded enzyme, some structural changes were observed around the active site. In the unliganded enzyme, Y216 serves as the fifth ligand for the active site zinc ion. On ligand binding, Y216 may move to form a hydrogen-bond with the carbonyl oxygen of the P1 residue of a ligand peptide. D191 in the flexible loop, Y190 to D196, over the active site cleft forms hydrogen-bonds with the backbone atoms of the P1 and P2 residues of the ligand to close the entrance of the cleft. The water molecule which is the fourth ligand for the zinc ion is replaced by the carbonyl oxygen of the P1 residue. These structural changes around the active site may reflect the substrate-binding mode during the enzymatic reaction.

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