1ept: Difference between revisions

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New page: left|200px<br /><applet load="1ept" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ept, resolution 1.8Å" /> '''REFINED 1.8 ANGSTROMS...
 
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[[Image:1ept.gif|left|200px]]<br /><applet load="1ept" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1ept.gif|left|200px]]<br /><applet load="1ept" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1ept, resolution 1.8&Aring;" />
caption="1ept, resolution 1.8&Aring;" />
'''REFINED 1.8 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF PORCINE EPSILON-TRYPSIN'''<br />
'''REFINED 1.8 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF PORCINE EPSILON-TRYPSIN'''<br />


==Overview==
==Overview==
Porcine epsilon-trypsin is a three-chain inactivated trypsin from the, limited autolysis of porcine beta-trypsin. It is cleaved at positions, Lys60-Ser61 and Lys145-Ser146. The crystal structure has been determined, by using the molecular replacement method, and refined at 1.8 A, resolution. The R-value of final model is 0.184. Comparison with the, electron density map of porcine beta-trypsin (PTRY) in complex (BBIT), and, with that of native bovine beta-trypsin (HTNA), revealed no obvious, changes except at the autolysis positions, and no changes at the active, center were observed. The autolysis at positions Lys60-Ser61 and, Lys145-Ser146 does not affect the conformation of His-57 in the active, center and therefore cannot explain for a loss in porcine epsilon-trypsin, activity.
Porcine epsilon-trypsin is a three-chain inactivated trypsin from the limited autolysis of porcine beta-trypsin. It is cleaved at positions Lys60-Ser61 and Lys145-Ser146. The crystal structure has been determined by using the molecular replacement method, and refined at 1.8 A resolution. The R-value of final model is 0.184. Comparison with the electron density map of porcine beta-trypsin (PTRY) in complex (BBIT), and with that of native bovine beta-trypsin (HTNA), revealed no obvious changes except at the autolysis positions, and no changes at the active center were observed. The autolysis at positions Lys60-Ser61 and Lys145-Ser146 does not affect the conformation of His-57 in the active center and therefore cannot explain for a loss in porcine epsilon-trypsin activity.


==About this Structure==
==About this Structure==
1EPT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EPT OCA].  
1EPT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EPT OCA].  


==Reference==
==Reference==
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[[Category: hydrolase (serine protease)]]
[[Category: hydrolase (serine protease)]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:12:53 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:30:17 2008''