Mitochondria can recognize and assemble fragments of a β-barrel structure

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Mitochondria can recognize and assemble fragments of a β-barrel structure

β-barrel proteins are found in the outer membranes of eukaryotic organelles of endosymbiotic origin as well as in the outer membrane of Gram-negative bacteria. Precursors of mitochondrial β-barrel proteins are synthesized in the cytosol and have to be targeted to the organelle. Currently, the signal that assures their specific targeting to mitochondria is poorly defined. To characterize the str...

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Functional fragments of disorder in outer membrane β barrel proteins

The traditional view of "sequence-structure-function" has been amended by the discovery of intrinsically disordered proteins. Almost 50% of PDB structures are now known to have one or more regions of disorder, which are involved in diverse functions. These regions typically possess low aromatic content and sequence complexity as well as high net charge and flexibility. In this study, we examine...

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TMBpro: Secondary Structure, β-contact, and Tertiary Structure Prediction of Transmembrane β-Barrel Proteins

Motivation: Transmembrane -barrel (TMB) proteins are embedded in the outer membranes of mitochondria, Gram-negative bacteria, and chloroplasts. These proteins perform critical functions, including active ion-transport and passive nutrient intake. Therefore there is a need for accurate prediction of secondary and tertiary structure of TMB proteins. Traditional homology modeling methods, however,...

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Structure and Assembly of β-Barrel Membrane Proteins

Integral membrane proteins fall into two major structural classes; they consist of individual or bundled TM -helices, or they form monomeric, dimeric, or trimeric TM -barrels. These folds are dictated by the necessity to form oriented hydrogenbonded secondary structures in the highly ordered apolar environment of the lipid bilayer. No other structural motif has yet been confirmed for membrane p...

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ژورنال

عنوان ژورنال: Molecular Biology of the Cell

سال: 2011

ISSN: 1059-1524,1939-4586

DOI: 10.1091/mbc.e10-12-0943