1akl

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{{STRUCTURE_1akl| PDB=1akl | SCENE= }}
{{STRUCTURE_1akl| PDB=1akl | SCENE= }}
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'''ALKALINE PROTEASE FROM PSEUDOMONAS AERUGINOSA IFO3080'''
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===ALKALINE PROTEASE FROM PSEUDOMONAS AERUGINOSA IFO3080===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_8690704}}
==About this Structure==
==About this Structure==
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[[Category: Miyatake, H.]]
[[Category: Miyatake, H.]]
[[Category: Morihara, K.]]
[[Category: Morihara, K.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:02:42 2008''

Revision as of 14:02, 30 June 2008

Template:STRUCTURE 1akl

ALKALINE PROTEASE FROM PSEUDOMONAS AERUGINOSA IFO3080

Template:ABSTRACT PUBMED 8690704

About this Structure

1AKL is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.

Reference

Crystal structure of the unliganded alkaline protease from Pseudomonas aeruginosa IFO3080 and its conformational changes on ligand binding., Miyatake H, Hata Y, Fujii T, Hamada K, Morihara K, Katsube Y, J Biochem. 1995 Sep;118(3):474-9. PMID:8690704

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