1AKL

ALKALINE PROTEASE FROM PSEUDOMONAS AERUGINOSA IFO3080

Summary for 1AKL

• Entry DOI: 10.2210/pdb1akl/pdb
• Descriptor: ALKALINE PROTEASE, ZINC ION, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: hydrolase (metalloproteinase)
• Biological source: Pseudomonas aeruginosa
• Cellular location: Secreted: Q03023
• Total number of polymer chains: 1
• Total formula weight: 49917.46

Authors

Miyatake, H.,Hata, Y.,Fujii, T.,Hamada, K.,Morihara, K.,Katsube, Y. (deposition date: 1995-09-16, release date: 1996-03-08, Last modification date: 2024-02-07)

Primary citation

Miyatake, H.,Hata, Y.,Fujii, T.,Hamada, K.,Morihara, K.,Katsube, Y.
Crystal structure of the unliganded alkaline protease from Pseudomonas aeruginosa IFO3080 and its conformational changes on ligand binding.
J.Biochem.(Tokyo), 118:474-479, 1995

PubMed Abstract: The crystal structure of the unliganded alkaline protease from Pseudomonas aeruginosa IFO3080 has been determined at 2.0 A resolution by the X-ray method. The enzyme consists of N-terminal catalytic and C-terminal beta-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 to 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.

PubMed: 8690704

Experimental method

X-RAY DIFFRACTION (2 Å)