1akl
From Proteopedia
(New page: 200px<br /><applet load="1akl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1akl, resolution 2.0Å" /> '''ALKALINE PROTEASE FRO...) |
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| - | [[Image:1akl.gif|left|200px]]<br /><applet load="1akl" size=" | + | [[Image:1akl.gif|left|200px]]<br /><applet load="1akl" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1akl, resolution 2.0Å" /> | caption="1akl, resolution 2.0Å" /> | ||
'''ALKALINE PROTEASE FROM PSEUDOMONAS AERUGINOSA IFO3080'''<br /> | '''ALKALINE PROTEASE FROM PSEUDOMONAS AERUGINOSA IFO3080'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the unliganded alkaline protease from Pseudomonas | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1AKL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with ZN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Serralysin Serralysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.40 3.4.24.40] Full crystallographic information is available from [http:// | + | 1AKL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Serralysin Serralysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.40 3.4.24.40] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AKL OCA]. |
==Reference== | ==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 | + | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8690704 8690704] |
[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Serralysin]] | [[Category: Serralysin]] | ||
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[[Category: hydrolase (metalloproteinase)]] | [[Category: hydrolase (metalloproteinase)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:45:33 2008'' |
Revision as of 09:45, 21 February 2008
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ALKALINE PROTEASE FROM PSEUDOMONAS AERUGINOSA IFO3080
Overview
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.
About this Structure
1AKL is a Single protein structure of sequence from Pseudomonas aeruginosa with and as ligands. Active as Serralysin, with EC number 3.4.24.40 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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