Preliminary X-ray crystallographic studies of yeast mitochondrial protein Tom70p
| Autor: | Lisa Nagy, Yunkun Wu, Bingdong Sha, Lawrence J. DeLucas, Debbie McCombs |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Saccharomyces cerevisiae Proteins
biology Translocase of the outer membrane Biophysics Membrane Proteins TIM/TOM complex Crystallography X-Ray Condensed Matter Physics Mitochondrial carrier Mitochondrial Membrane Transport Proteins Biochemistry Protein Transport Mitochondrial membrane transport protein Crystallography Crystallization Communications Structural Biology Mitochondrial Precursor Protein Import Complex Proteins Translocase of the inner membrane Genetics biology.protein ATP–ADP translocase Crystallization Inner mitochondrial membrane Intermembrane space |
| Zdroj: | Acta Crystallographica Section F Structural Biology and Crystallization Communications. 62:265-267 |
| ISSN: | 1744-3091 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text