Structural highlights
Disease
AFG32_HUMAN Spinocerebellar ataxia type 28;Early-onset spastic ataxia-neuropathy syndrome. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
Function
AFG32_HUMAN ATP-dependent protease which is essential for axonal development (By similarity).
Publication Abstract from PubMed
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.
NMR structure and MD simulations of the AAA protease intermembrane space domain indicates peripheral membrane localization within the hexaoligomer.,Ramelot TA, Yang Y, Sahu ID, Lee HW, Xiao R, Lorigan GA, Montelione GT, Kennedy MA FEBS Lett. 2013 Nov 1;587(21):3522-8. doi: 10.1016/j.febslet.2013.09.009. Epub, 2013 Sep 18. PMID:24055473[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ramelot TA, Yang Y, Sahu ID, Lee HW, Xiao R, Lorigan GA, Montelione GT, Kennedy MA. NMR structure and MD simulations of the AAA protease intermembrane space domain indicates peripheral membrane localization within the hexaoligomer. FEBS Lett. 2013 Nov 1;587(21):3522-8. doi: 10.1016/j.febslet.2013.09.009. Epub, 2013 Sep 18. PMID:24055473 doi:http://dx.doi.org/10.1016/j.febslet.2013.09.009
