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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 DOI10.2210/pdb2lna/pdb
NMR InformationBMRB: 18156
DescriptorAFG3-like protein 2 (1 entity in total)
Functional Keywordsstructural genomics, northeast structural genomics consortium (nesg), psi-biology, protein structure initiative, mpp, hydrolase, mitochondrial protein partnership
Biological sourceHomo sapiens (human)
Cellular locationMitochondrion membrane; Multi-pass membrane protein: Q9Y4W6
Total number of polymer chains1
Total formula weight11493.87
Authors
Primary citationRamelot, 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: 24055473
DOI: 10.1016/j.febslet.2013.09.009
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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