NMR solution structure of SlyD from Escherichia coli: spatial separation of prolyl isomerase and chaperone function.

Abstract

SlyD (sensitive to lysis D) is a putative folding helper from the bacterial cytosol and harbors prolyl isomerase and chaperone activities. We determined the solution NMR structure of a truncated version of SlyD (1-165) from Escherichia coli (SlyD*) that lacks the presumably unstructured C-terminal tail. SlyD* consists of two well-separated domains: the FKBP… (More)
DOI: 10.1016/j.jmb.2009.01.034

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Cite this paper

@article{Weininger2009NMRSS, title={NMR solution structure of SlyD from Escherichia coli: spatial separation of prolyl isomerase and chaperone function.}, author={Ulrich Weininger and Caroline Haupt and Kristian Schweimer and Wenke Graubner and Michael Kovermann and Thomas Br{\"{u}ser and Christian Wilfried Scholz and Peter Schaarschmidt and Gabriel Žold{\'a}k and Franz Xaver Schmid and Jochen Balbach}, journal={Journal of molecular biology}, year={2009}, volume={387 2}, pages={295-305} }