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2GW1

Crystal Structure of the Yeast Tom70

Summary for 2GW1
Entry DOI10.2210/pdb2gw1/pdb
DescriptorMitochondrial precursor proteins import receptor (2 entities in total)
Functional Keywordstpr, protein transport
Biological sourceSaccharomyces cerevisiae (baker's yeast)
Cellular locationMitochondrion outer membrane ; Single-pass membrane protein : P07213
Total number of polymer chains2
Total formula weight117620.42
Authors
Wu, Y.,Sha, B. (deposition date: 2006-05-03, release date: 2006-06-27, Last modification date: 2024-11-13)
Primary citationWu, Y.,Sha, B.
Crystal structure of yeast mitochondrial outer membrane translocon member Tom70p.
Nat.Struct.Mol.Biol., 13:589-593, 2006
Cited by
PubMed Abstract: A majority of the proteins targeted to the mitochondria are transported through the translocase of the outer membrane (TOM) complex. Tom70 is a major surface receptor for mitochondrial protein precursors in the TOM complex. To investigate how Tom70 receives the mitochondrial protein precursors, we have determined the crystal structure of yeast Tom70p to 3.0 A. Tom70p forms a homodimer in the crystal. Each subunit consists primarily of tetratricopeptide repeat (TPR) motifs, which are organized into a right-handed superhelix. The TPR motifs in the N-terminal domain of Tom70p form a peptide-binding groove for the C-terminal EEVD motif of Hsp70, whereas the C-terminal domain of Tom70p contains a large pocket that may be the binding site for mitochondrial precursors. The crystal structure of Tom70p provides insights into the mechanisms of precursor transport across the mitochondrion's outer membrane.
PubMed: 16767096
DOI: 10.1038/nsmb1106
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

229380

数据于2024-12-25公开中

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