Premium
NMR structure and MD simulations of the AAA protease intermembrane space domain indicates peripheral membrane localization within the hexaoligomer
Author(s) -
Ramelot Theresa A.,
Yang Yunhuang,
Sahu Indra D.,
Lee Hsiau-Wei,
Xiao Rong,
Lorigan Gary A.,
Montelione Gaetano T.,
Kennedy Michael A.
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.09.009
Subject(s) - intermembrane space , biophysics , protease , chemistry , mitochondrial intermembrane space , inner mitochondrial membrane , cryo electron microscopy , aaa proteins , inner membrane , crystallography , membrane , biochemistry , microbiology and biotechnology , biology , atpase , bacterial outer membrane , enzyme , escherichia coli , gene
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.