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Biochemical studies investigating transport proteins in the bacterial outer membrane, the outer component of the cell envelope of Gram negative bacteria, along with the role of chaperones in the folding and assembly of outer membrane proteins.

Structure and assembly of the LamB protein, the maltoporin in the outer membrane of Escherichia coli: folding studies of purified LamB protein and mutant proteins, and dissociation and reassociation of the LamB trimer.

• Luckey, et al., Journal of Bacteriology 111, 731-738, 1972.
  
  • As a graduate student working with J. B. Neilands, I wrote the first paper indicating that enteric bacteria have the ability to specifically utilize siderophores (iron chelates) produced and secreted by other microorganisms. This was a seminal paper: at present there are hundreds of papers published on these uptake systems.
• Luckey, et al., BBRC 64, 687-693, 1975.
• For my Ph.D. thesis, I showed that a partially purified outer membrane protein (then called TonA, now called FhuA) could bind to ferrichrome in vitro, providing the first evidence for the role of this phage and colicin receptor in iron transport in Escherichia coli. Many studies of this protein followed, including the recent solution of its crystal structure.
• Luckey and Nikaido, PNAS 77, 167-171, 1980.
  • As a postdoc in the lab of Hiroshi Nikaido, I purified the LamB protein from the outer membrane of E. coli and showed that it was specific for the uptake of maltose and maltodextrins when reconstituted in proteoliposomes. While controversial at the time, my results were later confirmed by conductance studies; these data are included in Garrett and Grisham, Biochemistry, 2nd edition page 314. They were further confirmed by X-ray crystallography of the LamB protein in the presence of various substrates as described in J. Mol. Biol. 272, 56-63, 1997.
• Luckey and Nikaido, BBRC 93, 166-171, 1980.
  • Using larger maltodextrins to inhibit the uptake of glucose and maltose in the LamB protein channels in reconstituted liposomes, I was able to measure a Ki of ca.1 mM for maltoheptaose and maltohexaose. Since traditional measurements did not detect direct binding of substrates to LamB protein, this established the specific but weak affinity of the protein for its substrates, which is consistent with its role in mediating passive diffusion of maltodextrins.
• Luckey et al., JBC 266, 1866-1871, 1991.
  • With students at SFSU, we proved that the two cysteinyl residues of LamB protein make an intrasubunit disulfide that is not essential for function but is required for the unusual thermal stability of the trimer in Triton X-100. Also we observed a high mobility band on SDS polyacrylamide gels when purified LamB protein is acidified, and used in situ proteolysis to prove the band is indeed a form of LamB protein.
• Unpublished results
  • We have characterized the low pH species of LamB protein as a compact monomer that reassembles to trimer when neutralized. After eluting the low pH species from a gel, we found this material has the circular dichroism spectrum of the native trimer indicative of a β-barrel structure. Prepublication reports of this work enabled Rouviere and Gross to identify this band when observed as an assembly intermediate in vivo.

• Iron uptake in Salmonella typhimurium:  Utilization of exogenous siderochromes as iron carriers.  1972.  M. Luckey, J. Pollack, R. Wayne, B. N. Ames and J. B. Neilands, Journal of Bacteriology 111, 731-738.
• In vitro competition between ferrichrome and phage for the outer membrane T5 receptor complex of Escherichia coli.  1975.  M. Luckey, R. Wayne and J. B. Neilands, Biochemical and Biophysical Research Communications 64, 687-693.
• Specificity of diffusion channels produced by the lambda receptor protein of Escherichia coli. 1980.  M. Luckey and H. Nikaido, Proc. Natl. Acad. Sci. 77, 167-171.
• Diffusion of solutes through channels produced by phage lambda receptor protein of Escherichia coli:  Inhibition by higher oligosaccharides of maltose series.  1980.  M. Luckey and H. Nikaido, Biochem. Biophys. Res. Commun. 93, 166-171.
• Non-specific and specific diffusion channels in the outer membrane of Escherichia coli.  1980.  H. Nikaido, M. Luckey and E. Y. Rosenberg, J. of Supramol. Str. 13, 305-313.
• Role of a disulfide bond in the thermal stability of the LamB protein trimer in Escherichia coli outer membrane.  1991.  M. Luckey, R. Ling, A. Dose and B. Malloy, J. Biol. Chem. 266, 1866-1871.
• Structural and Functional Characterization of OmpF Porin Mutants Selected for Larger Pore Size, II. Functional Characterization.  1996.  N. Saint, K.L. Lou, C. Widmer, M. Luckey, T. Schirmer and J.P. Rosenbusch. J. Biological Chemistry, 271, 20676-20680.
• Author of new textbook:
  Membrane Structural Biology with Biochemical and Biophysical Foundations, Cambridge University Press, 2008.

• National Institutes of Health, New Investigator Research Award, Transport Mechanism of LamB Protein in Escherichia coli, 12/1/83-5/30/87, $97,500.
• National Science Foundation Research Instrumentation Award, Centrifuge Facility for Biochemistry Research, M. Luckey, P.I. with W. Z. Plachy and D. Eden, 1/1/85-12/31/85, $77,511.
• National Science Foundation Chemical Instrumentation Program, High Performance Liquid Chromatography Instrumentation for Chemical and Biochemical Research, M. Luckey, co-P.I. with J. Orenberg, P.I., F. A. Walker and D. Eden, 9/1/85-8/31/86, $30,000.
• National Institutes of Health, DRR-BRS Shared Instrumentation Grant, Request for GE-Nicolet GN-300 NMR Spectrometer, M. Luckey, Co-P.I. with F. A. Walker, P.I., et al., 12/1/85-11/30/86, $427,196.
• National Science Foundation Biological Instrumentation Program, Purchase of a Nuclear Magnetic Resonance Spectrometer, M. Luckey, Co.-P.I., with F. A. Walker, P.I., et al., 12/1/85-11/30/86, $156,000.
• National Institutes of Health Research Career Development Award, LamB Protein Transport Channel in E. coli Outer Membrane, 2/1/87-1/31/92, $217,031.
• National Institutes of Health AREA Award, Heat Shock Proteins of the E. coli cell envelope, 6/1/93 - 5/30/96, $108,662.
• National Institutes of Health AREA Award, Do Chaperones Aid LamB Assembly in E. coli Cell Envelope, 8/1/96-7/31/99, $112,034.