2VU8

Crystal structure of an insect inhibitor with a fungal trypsin

2VU8 の概要

• エントリーDOI: 10.2210/pdb2vu8/pdb
• 関連するPDBエントリー: 1FN8 1FY4 1FY5 1GDN 1GDQ 1GDU 1PPZ 1PQ5 1PQ7 1PQ8 1PQA 1TRY 1WO9 1XVM 1XVO
• 分子名称: TRYPSIN, PACIFASTIN-RELATED SERINE PROTEASE INHIBITOR (3 entities in total)
• 機能のキーワード: hydrolase/inhibitor, canonical inhibitor, inhibitor, serine protease, species selectivity, insect, zymogen, protease, secreted, hydrolase, hydrolase-inhibitor complex
• 由来する生物種: FUSARIUM OXYSPORUM (MOLD); 詳細
• 細胞内の位置: Secreted: P35049
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 25799.62

構造登録者

Leone, P.,Roussel, A.,Kellenberger, C. (登録日: 2008-05-21, 公開日: 2008-12-23, 最終更新日: 2024-11-06)

主引用文献

Leone, P.,Roussel, A.,Kellenberger, C.
Structure of Locusta Migratoria Protease Inhibitor 3 (Lmpi-3) in Complex with Fusarium Oxysporum Trypsin.
Acta Crystallogr.,Sect.D, 64:1165-, 2008

PubMed Abstract: Previous studies have shown that the trypsin inhibitors LMPI-1, LMPI-3 and SGTI from locusts display an unusual species selectivity. They inhibit locust, crayfish and fungal trypsins several orders of magnitude more efficiently than bovine trypsin. In contrast, the chymotrypsin inhibitors from the same family, LMPI-2 and SGCI, are active towards mammalian enzymes. The crystal structures of a variant of LMPI-1 and of LMPI-2 in complex with bovine chymotrypsin have revealed subtle structural differences between the trypsin and chymotrypsin inhibitors. In a previous report, it was proposed that Pro173 of bovine trypsin is responsible for the weak inhibitory activity of LMPI-1 and LMPI-3. A fungal trypsin from Fusarium oxysporum contains Gly173 instead of Pro173 and has been shown to be strongly inhibited by LMPI-1 and LMPI-3. To explore the structural features that are responsible for this property, the crystal structure of the complex between LMPI-3 and F. oxysporum trypsin was determined at 1.8 A resolution. This study indicates that this small inhibitor interacts with the protease through the reactive site P3-P4' and the P10-P6 residues. Comparison of this complex with the SGTI-crayfish trypsin and BPTI-bovine trypsin complexes reinforces this hypothesis on the role of residue 173 of trypsin in species selectivity.

PubMed: 19020355
DOI: 10.1107/S0907444908030400

実験手法

X-RAY DIFFRACTION (1.8 Å)