Oral Sessions (Day1, Day2, Day3)
Poster Presentations (Day1, Day2, Day3)
Poster Presentations
- Day 1, June 22（Wed.） Room P (501, 502 and 503)
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1P-03 PDF
Analysis of the binding state of the intramembrane-cleaving protease RseP to zinc ion / inhibitor by native mass spectrometry
Native mass spectrometry (MS) is recognized as an effective tool for analysis of membrane proteins. However, native mass spectrometry of membrane proteins is extremely difficult. The intramembrane-cleaving protease RseP is a four-transmembrane protein and retains a zinc ion in its active center. Most recently, the crystal structures of inhibitor-bound forms of RseP from E. coli (EcRseP) and its ortholog from marine bacterium Kangiella koreensis (KkRseP) have been elucidated. Although the two orthologs had high sequence homology and similar domain structures, there were differences in structural properties near the active center. In this study, we attempted to observe two species of orthologs of EcRseP and KkRseP in the intact state and in the complex form with an inhibitor by native MS. By quantitatively comparing the binding states of the active center with zinc ion and inhibitor, we have gained insights into the differences in structural properties near the active center.