| The model of interactions presented suggests a way that binding between SecA and SecB might decrease the affinity of precursor polypeptides for SecB and facilitate the transfer to SecA. | The basis of asymmetry in the SecA:SecB complex.
Suo Y, Hardy SJS, Randall LL., Free PMC Article | 05/2/2015 |
| Demonstrated directly an interaction between the N-terminal residues 2 through 11 of SecA and the C-terminal 13 residues of SecB by isothermal titration calorimetry and analytical sedimentation velocity centrifugation. | Direct identification of the site of binding on the chaperone SecB for the amino terminus of the translocon motor SecA.
Randall LL, Henzl MT., Free PMC Article | 09/6/2010 |
| the structure of the SecB/OmpA complex was visualized by electron microscopy. The binding pattern between SecB tetramer and OmpA is asymmetric. | The structure of SecB/OmpA as visualized by electron microscopy: The mature region of the precursor protein binds asymmetrically to SecB.
Tang Y, Pan X, Tai PC, Sui SF. | 05/3/2010 |
| SecB exhibits the remarkable ability to bind a diverse group of ligands recognizing them by virtue of the fact that they have non-native structure. | Export chaperone SecB uses one surface of interaction for diverse unfolded polypeptide ligands.
Lilly AA, Crane JM, Randall LL., Free PMC Article | 01/21/2010 |
| Variants of SecA and of SecB that populate complexes were used to examine both the hydrolysis of ATP and the translocation of polypeptides. | Maximal efficiency of coupling between ATP hydrolysis and translocation of polypeptides mediated by SecB requires two protomers of SecA.
Mao C, Hardy SJ, Randall LL., Free PMC Article | 01/21/2010 |
| effect of chaperone SecB on folding & unfolding pathways of maltose binding protein at the single-molecule level; interactions with SecB prevent stable tertiary contacts in core structure but have no detectable effect on folding of external alpha helices | Direct observation of chaperone-induced changes in a protein folding pathway.
Bechtluft P, van Leeuwen RG, Tyreman M, Tomkiewicz D, Nouwen N, Tepper HL, Driessen AJ, Tans SJ. | 01/21/2010 |
| N-terminus verified by Edman degradation on mature peptide | Purification of the Escherichia coli secB gene product and demonstration of its activity in an in vitro protein translocation system.
Kumamoto CA, Chen L, Fandl J, Tai PC. | 11/5/2007 |
| structural details of SecA on lipid layers; the pore structure is altered after transferring crystals to the SecB solution, indicating that the lipid-specific SecA structure has the SecB binding activity. | The active ring-like structure of SecA revealed by electron crystallography: conformational change upon interaction with SecB.
Chen Y, Tai PC, Sui SF., Free PMC Article | 01/21/2010 |
| SecB and SecA display twofold symmetry and yet the complex between the two is stabilized by contacts that are distributed asymmetrically, we identify a third distinct region of their interaction | Characterization of three areas of interactions stabilizing complexes between SecA and SecB, two proteins involved in protein export.
Patel CN, Smith VF, Randall LL., Free PMC Article | 01/21/2010 |
| binding between the two symmetric molecules is asymmetric and that the C-terminal alpha-helices of SecB bind in the interfacial region of the SecA dimer | Asymmetric binding between SecA and SecB two symmetric proteins: implications for function in export.
Randall LL, Crane JM, Lilly AA, Liu G, Mao C, Patel CN, Hardy SJ. | 01/21/2010 |
| the primary role of SecB is to facilitate the targeting of secretory proteins to the Sec-translocase | Defining the role of the Escherichia coli chaperone SecB using comparative proteomics.
Baars L, Ytterberg AJ, Drew D, Wagner S, Thilo C, van Wijk KJ, de Gier JW. | 01/21/2010 |
| SecB residues involved in contacts with the unfolded form of bound precursor, galactose-binding protein, are identified as those that upon addition of the unfolded polypeptide ligand show changes in spectral line shape. | Sites of interaction of a precursor polypeptide on the export chaperone SecB mapped by site-directed spin labeling.
Crane JM, Suo Y, Lilly AA, Mao C, Hubbell WL, Randall LL., Free PMC Article | 01/21/2010 |