2vu8

Crystal structure of an insect inhibitor with a fungal trypsin

spinqualitylabelsall models 2vu8, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2vu8 is a 2 chain structure with sequence from Fusarium oxysporum and Locusta migratoria. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TRYP_FUSOX Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structure of Locusta migratoria protease inhibitor 3 (LMPI-3) in complex with Fusarium oxysporum trypsin.,Leone P, Roussel A, Kellenberger C Acta Crystallogr D Biol Crystallogr. 2008 Nov;64(Pt 11):1165-71. Epub 2008, Oct 18. PMID:19020355 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Trypsin 3D structures

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