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)

Summary for 1OM2

• Entry DOI: 10.2210/pdb1om2/pdb
• NMR Information: BMRB: 4496
• Descriptor: PROTEIN (MITOCHONDRIAL IMPORT RECEPTOR SUBUNIT TOM20), PROTEIN (MITOCHONDRIAL ALDEHYDE DEHYDROGENASE) (2 entities in total)
• Functional Keywords: mitochondrial protein import across outer membrane, receptor for presequences, mitochondrial targeting signal, presequence peptide, receptor-oxidoreductase complex complex, receptor/oxidoreductase complex
• Biological source: Rattus norvegicus (Norway rat); More
• Cellular location: Mitochondrion outer membrane; Single-pass membrane protein (Potential): Q62760; Mitochondrion matrix: P11884
• Total number of polymer chains: 2
• Total formula weight: 11697.36

Authors

Abe, Y.,Shodai, T.,Muto, T.,Mihara, K.,Torii, H.,Nishikawa, S.,Endo, T.,Kohda, D. (deposition date: 1999-04-23, release date: 2000-02-02, Last modification date: 2023-12-27)

Primary citation

Abe, Y.,Shodai, T.,Muto, T.,Mihara, K.,Torii, H.,Nishikawa, S.,Endo, T.,Kohda, D.
Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20.
Cell(Cambridge,Mass.), 100:551-560, 2000

PubMed Abstract: 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.

PubMed: 10721992
DOI: 10.1016/S0092-8674(00)80691-1

Experimental method

SOLUTION NMR