1ept
From Proteopedia
(New page: 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=" | + | [[Image:1ept.gif|left|200px]]<br /><applet load="1ept" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ept, resolution 1.8Å" /> | caption="1ept, resolution 1.8Å" /> | ||
'''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 | + | 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:// | + | 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:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:30:17 2008'' |
Revision as of 10:30, 21 February 2008
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REFINED 1.8 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF PORCINE EPSILON-TRYPSIN
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.
About this Structure
1EPT is a Protein complex structure of sequences from Sus scrofa with as ligand. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.
Reference
Refined 1.8 A resolution crystal structure of the porcine epsilon-trypsin., Huang Q, Wang Z, Li Y, Liu S, Tang Y, Biochim Biophys Acta. 1994 Nov 16;1209(1):77-82. PMID:7947985
Page seeded by OCA on Thu Feb 21 12:30:17 2008
Categories: Protein complex | Sus scrofa | Trypsin | Huang, Q. | Li, Y. | Liu, S. | Tang, Y. | Wang, Z. | CA | Hydrolase (serine protease)
