1e5t

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[[Image:1e5t.jpg|left|200px]]<br /><applet load="1e5t" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1e5t.jpg|left|200px]]
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caption="1e5t, resolution 1.7&Aring;" />
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'''PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT'''<br />
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{{Structure
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|PDB= 1e5t |SIZE=350|CAPTION= <scene name='initialview01'>1e5t</scene>, resolution 1.7&Aring;
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|SITE= <scene name='pdbsite=AS:Active+Site,+Catalytic+Triad'>AS</scene> and <scene name='pdbsite=SS:Disulfide+Engineered+Between+Cys78+And+Gln397cys'>SS</scene>
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|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]
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|GENE=
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}}
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'''PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1E5T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Known structural/functional Sites: <scene name='pdbsite=AS:Active+Site,+Catalytic+Triad'>AS</scene> and <scene name='pdbsite=SS:Disulfide+Engineered+Between+Cys78+And+Gln397cys'>SS</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E5T OCA].
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1E5T 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=1E5T OCA].
==Reference==
==Reference==
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Catalysis of serine oligopeptidases is controlled by a gating filter mechanism., Fulop V, Szeltner Z, Polgar L, EMBO Rep. 2000 Sep;1(3):277-81. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11256612 11256612]
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Catalysis of serine oligopeptidases is controlled by a gating filter mechanism., Fulop V, Szeltner Z, Polgar L, EMBO Rep. 2000 Sep;1(3):277-81. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11256612 11256612]
[[Category: Prolyl oligopeptidase]]
[[Category: Prolyl oligopeptidase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: prolyl oligopeptidase]]
[[Category: prolyl oligopeptidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:24:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:50:10 2008''

Revision as of 08:50, 20 March 2008


PDB ID 1e5t

Drag the structure with the mouse to rotate
, resolution 1.7Å
Sites: and
Ligands:
Activity: Prolyl oligopeptidase, with EC number 3.4.21.26
Coordinates: save as pdb, mmCIF, xml



PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT


Overview

Proteases have a variety of strategies for selecting substrates in order to prevent uncontrolled protein degradation. A recent crystal structure determination of prolyl oligopeptidase has suggested a way for substrate selection involving an unclosed seven-bladed beta-propeller domain. We have engineered a disulfide bond between the first and seventh blades of the propeller, which resulted in the loss of enzymatic activity. These results provided direct evidence for a novel strategy of regulation in which oscillating propeller blades act as a gating filter during catalysis, letting small peptide substrates into the active site while excluding large proteins to prevent accidental proteolysis.

About this Structure

1E5T is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

Reference

Catalysis of serine oligopeptidases is controlled by a gating filter mechanism., Fulop V, Szeltner Z, Polgar L, EMBO Rep. 2000 Sep;1(3):277-81. PMID:11256612

Page seeded by OCA on Thu Mar 20 10:50:10 2008

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