1ept

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(New page: 200px<br /><applet load="1ept" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ept, resolution 1.8&Aring;" /> '''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"
 
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caption="1ept, resolution 1.8&Aring;" />
 
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'''REFINED 1.8 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF PORCINE EPSILON-TRYPSIN'''<br />
 
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==Overview==
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==REFINED 1.8 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF PORCINE EPSILON-TRYPSIN==
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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.
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<StructureSection load='1ept' size='340' side='right'caption='[[1ept]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ept]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EPT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EPT FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ept FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ept OCA], [https://pdbe.org/1ept PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ept RCSB], [https://www.ebi.ac.uk/pdbsum/1ept PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ept ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TRYP_PIG TRYP_PIG]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ep/1ept_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ept ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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<ref>PMID:7947985</ref>
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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].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7947985 7947985]
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</div>
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[[Category: Protein complex]]
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<div class="pdbe-citations 1ept" style="background-color:#fffaf0;"></div>
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[[Category: Sus scrofa]]
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[[Category: Trypsin]]
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[[Category: Huang, Q.]]
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[[Category: Li, Y.]]
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[[Category: Liu, S.]]
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[[Category: Tang, Y.]]
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[[Category: Wang, Z.]]
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[[Category: CA]]
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[[Category: hydrolase (serine protease)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:12:53 2007''
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==See Also==
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*[[Trypsin 3D structures|Trypsin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Sus scrofa]]
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[[Category: Huang Q]]
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[[Category: Li Y]]
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[[Category: Liu S]]
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[[Category: Tang Y]]
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[[Category: Wang Z]]

Current revision

REFINED 1.8 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF PORCINE EPSILON-TRYPSIN

PDB ID 1ept

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