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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Mar 1;62(Pt 3):265-7. Epub 2006 Feb 24.

Preliminary X-ray crystallographic studies of yeast mitochondrial protein Tom70p.

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Department of Cell Biology, Center for Biophysical Sciences and Engineering, University of Alabama, Birmingham, USA.


Protein translocations across mitochondrial membranes play critical roles in mitochondrion biogenesis. Protein transport from the cell cytosol to the mitochondrial matrix is carried out by the translocase of the outer membrane (TOM) complex and the translocase of the inner membrane (TIM) complexes. Tom70p is an important TOM-complex member and a major surface receptor of the protein-translocation machinery in the outer mitochondrial membrane. To investigate the mechanism by which Tom70p functions to deliver the mitochondrial protein precursors, the cytosolic fragment of yeast Tom70p (cTom70p) was crystallized. The crystals diffract to 3.2 A using a synchrotron X-ray source and belong to space group P2(1), with unit-cell parameters a = 44.89, b = 168.78, c = 83.41 A, alpha = 90.00, beta = 102.74, gamma = 90.00 degrees. There are two Tom70p molecules in one asymmetric unit, which corresponds to a solvent content of approximately 51%. Structure determination by MAD methods is under way.

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