2LNA
Solution NMR Structure of the mitochondrial inner membrane domain (residues 164-251), FtsH_ext, from the paraplegin-like protein AFG3L2 from Homo sapiens, Northeast Structural Genomics Consortium Target HR6741A
Summary for 2LNA
Entry DOI | 10.2210/pdb2lna/pdb |
NMR Information | BMRB: 18156 |
Descriptor | AFG3-like protein 2 (1 entity in total) |
Functional Keywords | structural genomics, northeast structural genomics consortium (nesg), psi-biology, protein structure initiative, mpp, hydrolase, mitochondrial protein partnership |
Biological source | Homo sapiens (human) |
Cellular location | Mitochondrion membrane; Multi-pass membrane protein: Q9Y4W6 |
Total number of polymer chains | 1 |
Total formula weight | 11493.87 |
Authors | Ramelot, T.A.,Yang, Y.,Lee, H.,Janua, H.,Kohan, E.,Shastry, R.,Acton, T.B.,Xiao, R.,Everett, J.K.,Prestegard, J.H.,Montelione, G.T.,Kennedy, M.A.,Northeast Structural Genomics Consortium (NESG),Mitochondrial Protein Partnership (MPP) (deposition date: 2011-12-20, release date: 2012-01-25, Last modification date: 2024-05-15) |
Primary citation | Ramelot, T.A.,Yang, Y.,Sahu, I.D.,Lee, H.W.,Xiao, R.,Lorigan, G.A.,Montelione, G.T.,Kennedy, M.A. NMR structure and MD simulations of the AAA protease intermembrane space domain indicates peripheral membrane localization within the hexaoligomer. Febs Lett., 587:3522-3528, 2013 Cited by PubMed 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. PubMed: 24055473DOI: 10.1016/j.febslet.2013.09.009 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
Download full validation report