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FEBS Lett. 2013 Nov 1;587(21):3522-8. doi: 10.1016/j.febslet.2013.09.009. Epub 2013 Sep 18.

NMR structure and MD simulations of the AAA protease intermembrane space domain indicates peripheral membrane localization within the hexaoligomer.

Author information

1
Department of Chemistry and Biochemistry, Northeast Structural Genomics Consortium, Miami University, Oxford, OH 45056, USA. Electronic address: theresa.ramelot@miamiOH.edu.

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:

Molecular dynamics; NMR structure; m-AAA protease

PMID:
24055473
PMCID:
PMC4043124
DOI:
10.1016/j.febslet.2013.09.009
[Indexed for MEDLINE]
Free PMC Article
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