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J. Biochem, 1995, Vol. 118, No. 3 474-479
© 1995 Japanese Biochemical Society

other

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

Hideyuki Miyatake*, Yasuo Hata*,2, Tomomi Fujii*, Kensaku Hamada{dagger}, Kazuyuki Morihara{ddagger} and Yukiteru Katsube§

*Institute for Chemical Research, Kyoto University Uji, Kyoto 611
{dagger}Faculty of Science, Shimane University Matsue, Shimane 690
{ddagger}Institute for Applied Life Science, University of East Asia 2-1 Ichinomiyoa-Gakuen-cho, Shimonoseki, Yamaguchi 751
§Institute for Protein Research, Osaka University Suita, Osaka 565

2To whom Correspondence should be addressed. Phone: +81-774-32-3111 (Ext. 2159), Fax: +81-774-33-1247

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 ß-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.

1 This work was supported in part by a Grant-in-Aid for Scientific Research on Priority Areas (No. 06235204) from the Ministry of Education, Science and Culture of Japan.


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