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Structural Analysis of Synthetic Peptide Fragments from EmrE, a Multidrug Resistance Protein, in a Membrane-Mimetic Environment

Venkatraman, Janani and Gowda, Nagana GA and Balaram, Padmanabhan (2002) Structural Analysis of Synthetic Peptide Fragments from EmrE, a Multidrug Resistance Protein, in a Membrane-Mimetic Environment. In: Biochemistry, 41 (21). pp. 6631-6639.

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EmrE, a multidrug resistance protein from Escherichia coli, renders the bacterium resistant to a variety of cytotoxic drugs by active translocation out of the cell. The 110-residue sequence of EmrE limits the number of structural possibilities that can be envisioned for this membrane protein. Four helix bundle models have been considered [Yerushalmi, H., Lebendiker, M., and Schuldiner, S. (1996) J. Biol. Chem. 271, 31044-31048]. The validity of EmrE structural models has been probed experimentally by investigations on overlapping peptides (ranging in length from 19 to 27 residues), derived from the sequence of EmrE. The choice of peptides was made to provide sequences of two complete, predicted transmembrane helices (peptides H1 and H3) and two helix-loop-helix motifs (peptides A and B). Peptide (B) also corresponds to a putative hairpin in a speculative ‚-barrel model, with the Pro-Thr-Gly segment forming a turn. Structure determination in SDS micelles using NMR indicates peptide H1 to be predominantly helical, with helix boundaries in the micellar environment corroborating predicted helical limits. Peptide A adopts a helix-loop-helix structure in SDS micelles, and peptide B was also largely helical in micellar environments. An analogue peptide, C, in which the central Pro-Thr-Gly was replaced by DPro-Gly displays local turn conformation at the DPro-Gly segment, but neither a continuous helical stretch nor ‚beta-hairpin formation was observed. This study implies that the constraints of membrane and micellar environments largely direct the structure of transmembrane peptides and proteins and study of judiciously selected peptide fragments can prove useful in the structural elucidation of membrane proteins.

Item Type: Journal Article
Additional Information: Copyright for this article belongs to American Chemical Society
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Division of Chemical Sciences > Sophisticated Instruments Facility (Continued as NMR Research Centre)
Depositing User: M.K Anitha
Date Deposited: 25 Aug 2008
Last Modified: 19 Sep 2010 04:14
URI: http://eprints.iisc.ac.in/id/eprint/1292

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