1fon: Difference between revisions

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{{STRUCTURE_1fon|  PDB=1fon  |  SCENE=  }}  
{{STRUCTURE_1fon|  PDB=1fon  |  SCENE=  }}  


'''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===




==Overview==
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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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==About this Structure==
==About this Structure==
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[[Category: Serine protease]]
[[Category: Serine protease]]
[[Category: Truncated zymogen e]]
[[Category: Truncated zymogen e]]
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