1FON
CRYSTAL STRUCTURE OF BOVINE PROCARBOXYPEPTIDASE A-S6 SUBUNIT III, A HIGHLY STRUCTURED TRUNCATED ZYMOGEN E
1FON の概要
| エントリーDOI | 10.2210/pdb1fon/pdb |
| 分子名称 | PROCARBOXYPEPTIDASE A-S6 (2 entities in total) |
| 機能のキーワード | truncated zymogen e, serine protease |
| 由来する生物種 | Bos taurus (cattle) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 51767.80 |
| 構造登録者 | Pignol, D.C.,Gaboriaud, T.,Michon, B.,Kerfelec, B.,Chapus, C.,Fontecilla-Camps, J.C. (登録日: 1996-02-01, 公開日: 1996-10-14, 最終更新日: 2024-10-16) |
| 主引用文献 | Pignol, D.,Gaboriaud, C.,Michon, T.,Kerfelec, B.,Chapus, C.,Fontecilla-Camps, J.C. Crystal structure of bovine procarboxypeptidase A-S6 subunit III, a highly structured truncated zymogen E. EMBO J., 13:1763-1771, 1994 Cited by PubMed Abstract: 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. PubMed: 8168476主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.7 Å) |
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