1om2
|
SOLUTION NMR STRUCTURE OF THE MITOCHONDRIAL PROTEIN IMPORT RECEPTOR TOM20 FROM RAT IN A COMPLEX WITH A PRESEQUENCE PEPTIDE DERIVED FROM RAT ALDEHYDE DEHYDROGENASE (ALDH)
OverviewOverview
Most mitochondrial proteins are synthesized in the cytosol as precursor, proteins with a cleavable N-terminal presequence and are imported into, mitochondria. We report here the NMR structure of a general import, receptor, rat Tom20, in a complex with a presequence peptide derived from, rat aldehyde dehydrogenase. The cytosolic domain of Tom20 forms an all, alpha-helical structure with a groove to accommodate the presequence, peptide. The bound presequence forms an amphiphilic helical structure with, hydrophobic leucines aligned on one side to interact with a hydrophobic, patch in the Tom20 groove. Although the positive charges of the, presequence are essential for import ability, presequence binding to Tom20, is mediated mainly by hydrophobic rather than ionic interactions.
About this StructureAbout this Structure
1OM2 is a Protein complex structure of sequences from Rattus norvegicus. Active as Aldehyde dehydrogenase (NAD(+)), with EC number 1.2.1.3 Full crystallographic information is available from OCA.
ReferenceReference
Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20., Abe Y, Shodai T, Muto T, Mihara K, Torii H, Nishikawa S, Endo T, Kohda D, Cell. 2000 Mar 3;100(5):551-60. PMID:10721992
Page seeded by OCA on Tue Nov 20 23:00:00 2007