2gw1
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(New page: 200px<br /><applet load="2gw1" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gw1, resolution 3.00Å" /> '''Crystal Structure of...)
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Revision as of 09:18, 21 November 2007
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Crystal Structure of the Yeast Tom70
Overview
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.
About this Structure
2GW1 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystal structure of yeast mitochondrial outer membrane translocon member Tom70p., Wu Y, Sha B, Nat Struct Mol Biol. 2006 Jul;13(7):589-93. Epub 2006 Jun 11. PMID:16767096
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