Journal
FEBS LETTERS
Volume 587, Issue 21, Pages 3522-3528Publisher
WILEY
DOI: 10.1016/j.febslet.2013.09.009
Keywords
m-AAA protease; Molecular dynamics; NMR structure
Funding
- National Institute of General Medical Sciences Protein Structure Initiative - Biology (PSI-Biology) [U54-GM094597]
- NESG
- Mitochondrial Protein Partnership (MPP) [U01-GM094622]
- Ohio Supercomputer Center (OSC) [PMIU0117]
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [1305664] Funding Source: National Science Foundation
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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. (C) 2013 Published by Elsevier B. V. on behalf of the Federation of European Biochemical Societies.
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