1vz2
From Proteopedia
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| - | [[Image:1vz2.jpg|left|200px]] | + | [[Image:1vz2.jpg|left|200px]] |
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| - | '''PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, Y73C/V427C/C255T MUTANT''' | + | {{Structure |
| + | |PDB= 1vz2 |SIZE=350|CAPTION= <scene name='initialview01'>1vz2</scene>, resolution 2.2Å | ||
| + | |SITE= <scene name='pdbsite=AS1:Engineered+Disulphide+Bridge'>AS1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Prolyl_oligopeptidase Prolyl oligopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.26 3.4.21.26] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, Y73C/V427C/C255T MUTANT''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1VZ2 is a [ | + | 1VZ2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VZ2 OCA]. |
==Reference== | ==Reference== | ||
| - | Concerted structural changes in the peptidase and the propeller domains of prolyl oligopeptidase are required for substrate binding., Szeltner Z, Rea D, Juhasz T, Renner V, Fulop V, Polgar L, J Mol Biol. 2004 Jul 9;340(3):627-37. PMID:[http:// | + | Concerted structural changes in the peptidase and the propeller domains of prolyl oligopeptidase are required for substrate binding., Szeltner Z, Rea D, Juhasz T, Renner V, Fulop V, Polgar L, J Mol Biol. 2004 Jul 9;340(3):627-37. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15210359 15210359] |
[[Category: Prolyl oligopeptidase]] | [[Category: Prolyl oligopeptidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: serine protease]] | [[Category: serine protease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:49:56 2008'' |
Revision as of 12:49, 20 March 2008
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| , resolution 2.2Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Prolyl oligopeptidase, with EC number 3.4.21.26 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, Y73C/V427C/C255T MUTANT
Overview
Prolyl oligopeptidase contains a peptidase domain and its catalytic triad is covered by the central tunnel of a seven-bladed beta-propeller. This domain makes the enzyme an oligopeptidase by excluding large structured peptides from the active site. The apparently rigid crystal structure does not explain how the substrate can approach the catalytic groups. Two possibilities of substrate access were investigated: either blades 1 and 7 of the propeller domain move apart, or the peptidase and/or propeller domains move to create an entry site at the domain interface. Engineering disulfide bridges to the expected oscillating structures prevented such movements, which destroyed the catalytic activity and precluded substrate binding. This indicated that concerted movements of the propeller and the peptidase domains are essential for the enzyme action.
About this Structure
1VZ2 is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
Reference
Concerted structural changes in the peptidase and the propeller domains of prolyl oligopeptidase are required for substrate binding., Szeltner Z, Rea D, Juhasz T, Renner V, Fulop V, Polgar L, J Mol Biol. 2004 Jul 9;340(3):627-37. PMID:15210359
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