1fon: Difference between revisions

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-[[Image:1fon.gif|left|200px]]
- {{Structure
+==CRYSTAL STRUCTURE OF BOVINE PROCARBOXYPEPTIDASE A-S6 SUBUNIT III, A HIGHLY STRUCTURED TRUNCATED ZYMOGEN E==
-|PDB= 1fon |SIZE=350|CAPTION= <scene name='initialview01'>1fon</scene>, resolution 1.7&Aring;
+<StructureSection load='1fon' size='340' side='right'caption='[[1fon]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND=
+<table><tr><td colspan='2'>[[1fon]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FON OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FON FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
-|GENE=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fon OCA], [https://pdbe.org/1fon PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fon RCSB], [https://www.ebi.ac.uk/pdbsum/1fon PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fon ProSAT]</span></td></tr>
-|DOMAIN=
+</table>
-|RELATEDENTRY=
+== Function ==
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fon OCA], [http://www.ebi.ac.uk/pdbsum/1fon PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fon RCSB]</span>
+[https://www.uniprot.org/uniprot/CAC3_BOVIN CAC3_BOVIN] May protect procarboxypeptidase A against denaturation in the acidic environment of the ruminant duodenum.
-}}
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fo/1fon_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1fon ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Subunit III, a defective serine endopeptidase lacking the typical N-terminal hydrophobic dipeptide is secreted by the pancreas of ruminant species as part of the bovine ternary complex procarboxypeptidase A-S6. Two monoclinic crystal forms were obtained and subsequently used to solve its X-ray structure. The highest resolution model of subunit III was refined at 1.7 A resolution to a crystallographic R-factor of 18.4%, with r.m.s. bond deviations from ideality of 0.012 A. About 80% of the model presents the characteristic architecture of trypsin-like proteases. The remaining zones, however, have well-defined, unique conformations. The regions from residues 70 to 80 and from 140 to 155 present maximum distances of 16 and 18 A relative to serine proteases and zymogens. Comparisons with the structures of porcine elastase 1 and chymotrypsinogen A indicate that the specific binding pocket of subunit III adopts a zymogen-like conformation and thus provide a basis for its inactivity. In general, the structural analysis of subunit III strongly suggests that it corresponds to a truncated version of a new class of highly structured elastase-like zymogen molecules. Based on the structures of subunit III and elastase 1, it is concluded that large concerted movements are necessary for the activation of zymogen E.
-'''CRYSTAL STRUCTURE OF BOVINE PROCARBOXYPEPTIDASE A-S6 SUBUNIT III, A HIGHLY STRUCTURED TRUNCATED ZYMOGEN E'''
+Crystal structure of bovine procarboxypeptidase A-S6 subunit III, a highly structured truncated zymogen E.,Pignol D, Gaboriaud C, Michon T, Kerfelec B, Chapus C, Fontecilla-Camps JC EMBO J. 1994 Apr 15;13(8):1763-71. PMID:8168476<ref>PMID:8168476</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1fon" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-Subunit III, a defective serine endopeptidase lacking the typical N-terminal hydrophobic dipeptide is secreted by the pancreas of ruminant species as part of the bovine ternary complex procarboxypeptidase A-S6. Two monoclinic crystal forms were obtained and subsequently used to solve its X-ray structure. The highest resolution model of subunit III was refined at 1.7 A resolution to a crystallographic R-factor of 18.4%, with r.m.s. bond deviations from ideality of 0.012 A. About 80% of the model presents the characteristic architecture of trypsin-like proteases. The remaining zones, however, have well-defined, unique conformations. The regions from residues 70 to 80 and from 140 to 155 present maximum distances of 16 and 18 A relative to serine proteases and zymogens. Comparisons with the structures of porcine elastase 1 and chymotrypsinogen A indicate that the specific binding pocket of subunit III adopts a zymogen-like conformation and thus provide a basis for its inactivity. In general, the structural analysis of subunit III strongly suggests that it corresponds to a truncated version of a new class of highly structured elastase-like zymogen molecules. Based on the structures of subunit III and elastase 1, it is concluded that large concerted movements are necessary for the activation of zymogen E.
+*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-FON is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FON OCA].
+__TOC__
+</StructureSection>
-==Reference==
-Crystal structure of bovine procarboxypeptidase A-S6 subunit III, a highly structured truncated zymogen E., Pignol D, Gaboriaud C, Michon T, Kerfelec B, Chapus C, Fontecilla-Camps JC, EMBO J. 1994 Apr 15;13(8):1763-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8168476 8168476]
 [[Category: Bos taurus]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Chapus, C.]]
+[[Category: Chapus C]]
-[[Category: Fontecilla-Camps, J C.]]
+[[Category: Fontecilla-Camps JC]]
-[[Category: Gaboriaud, T.]]
+[[Category: Gaboriaud T]]
-[[Category: Kerfelec, B.]]
+[[Category: Kerfelec B]]
-[[Category: Michon, B.]]
+[[Category: Michon B]]
-[[Category: Pignol, D C.]]
+[[Category: Pignol DC]]
-[[Category: serine protease]]
-[[Category: truncated zymogen e]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:27:04 2008''