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Structural insight into OprD substrate specificity


OprD proteins form a large family of substrate-specific outer-membrane channels in Gram-negative bacteria. We report here the X-ray crystal structure of OprD from Pseudomonas aeruginosa, which reveals a monomeric 18-stranded β-barrel characterized by a very narrow pore constriction, with a positively charged basic ladder on one side and an electronegative pocket on the other side. The location of highly conserved residues in OprD suggests that the structure represents the general architecture of OprD channels.

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Figure 1: Structure of P. aeruginosa OprD.
Figure 2: Single-channel conductance of wild-type OprD and mutants.

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This work was supported by a Pew Scholar award and University of Massachusetts Medical School start-up funds (B.v.d.B.), and by Syracuse University start-up funds and US National Science Foundation grant DMR-0706517 (L.M.). We thank E. Hearn for critical reading of the manuscript, K. Akpalu for purification of OprD mutants, and A.J. Wolfe, C.P. Goodrich and K.R. Howard for their help with single-channel experiments. We also thank the staff members of beamlines X6A and X25 at the National Synchrotron Light Source for beamtime and assistance.

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S.B. cloned, purified and crystallized OprD; M.M.M. performed single-channel electrical recordings; D.R.P. worked on the early stages of the project; L.M. supervised and designed single-channel electrical recordings; B.v.d.B. determined the OprD structure, designed research and wrote the manuscript.

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Correspondence to Bert van den Berg.

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Supplementary Figures 1–3, Supplementary Table 1, Supplementary Methods (PDF 381 kb)

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Biswas, S., Mohammad, M., Patel, D. et al. Structural insight into OprD substrate specificity. Nat Struct Mol Biol 14, 1108–1109 (2007).

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