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NMR structure and MD simulations of the AAA protease intermembrane space domain indicates peripheral membrane localization within the hexaoligomer |
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| Authors: | Theresa A. Ramelot Yunhuang Yang Indra D. Sahu Hsiau-Wei Lee Rong Xiao Gary A. Lorigan Gaetano T. Montelione Michael A. Kennedy |
| Affiliation: | 1. Department of Chemistry and Biochemistry, Northeast Structural Genomics Consortium, Miami University, Oxford, OH 45056, USA;2. Complex Carbohydrate Research Center, Northeast Structural Genomics Consortium, University of Georgia, Athens, GA 30602, USA;3. Center for Advanced Biotechnology and Medicine, Department of Molecular Biology and Biochemistry, Northeast Structural Genomics Consortium, Rutgers, University, Piscataway, NJ 08854, USA;4. Department of Biochemistry, Robert Wood Johnson Medical School, Piscataway, NJ 08854, USA |
| Abstract: | We have determined the solution NMR structure of the intermembrane space domain (IMSD) of the human mitochondrial ATPase associated with various activities (AAA) protease known as AFG3-like protein 2 (AFG3L2). Our structural analysis and molecular dynamics results indicate that the IMSD is peripherally bound to the membrane surface. This is a modification to the location of the six IMSDs in a model of the full length yeast hexaoligomeric homolog of AFG3L2 determined at low resolution by electron cryomicroscopy [1]. The predicted protein–protein interaction surface, located on the side furthest from the membrane, may mediate binding to substrates as well as prohibitins. |
| Keywords: | m-AAA protease Molecular dynamics NMR structure |
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