1fon

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== Structural highlights ==
== Structural highlights ==
<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>
<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>
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</td></tr><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>
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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]] 1.7&#8491;</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=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>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CAC3_BOVIN CAC3_BOVIN]] May protect procarboxypeptidase A against denaturation in the acidic environment of the ruminant duodenum.
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[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1fon ConSurf].
</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="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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.
 
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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>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1fon" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chapus, C]]
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[[Category: Chapus C]]
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[[Category: Fontecilla-Camps, J C]]
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[[Category: Fontecilla-Camps JC]]
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[[Category: Gaboriaud, T]]
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[[Category: Gaboriaud T]]
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[[Category: Kerfelec, B]]
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[[Category: Kerfelec B]]
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[[Category: Michon, B]]
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[[Category: Michon B]]
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[[Category: Pignol, D C]]
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[[Category: Pignol DC]]
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[[Category: Serine protease]]
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[[Category: Truncated zymogen e]]
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Revision as of 11:15, 27 March 2024

CRYSTAL STRUCTURE OF BOVINE PROCARBOXYPEPTIDASE A-S6 SUBUNIT III, A HIGHLY STRUCTURED TRUNCATED ZYMOGEN E

PDB ID 1fon

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