Startseite The contribution of methionine to the stability of the Escherichia coli MetNIQ ABC transporter-substrate binding protein complex
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The contribution of methionine to the stability of the Escherichia coli MetNIQ ABC transporter-substrate binding protein complex

  • Phong T. Nguyen , Qi Wen Li , Neena S. Kadaba , Jeffrey Y. Lai , Janet G. Yang und Douglas C. Rees EMAIL logo
Veröffentlicht/Copyright: 23. März 2015
Biological Chemistry
Aus der Zeitschrift Biological Chemistry Band 396 Heft 9-10

Abstract

Despite the ubiquitous role of ATP-binding cassette (ABC) importers in nutrient uptake, only the Escherichia coli maltose and vitamin B12 ABC transporters have been structurally characterized in multiple conformations relevant to the alternating access transport mechanism. To complement our previous structure determination of the E. coli MetNI methionine importer in the inward facing conformation (Kadaba et al. (2008) Science 321, 250–253), we have explored conditions stabilizing the outward facing conformation. Using two variants, the Walker B E166Q mutation with ATP+EDTA to stabilize MetNI in the ATP-bound conformation and the N229A variant of the binding protein MetQ, shown in this work to disrupt methionine binding, a high affinity MetNIQ complex was formed with a dissociation constant measured to be 27 nm. Using wild type MetQ containing a co-purified methionine (for which the crystal structure is reported at 1.6 Å resolution), the dissociation constant for complex formation with MetNI is measured to be ∼40-fold weaker, indicating that complex formation lowers the affinity of MetQ for methionine by this amount. Preparation of a stable MetNIQ complex is an essential step towards the crystallographic analysis of the outward facing conformation, a key intermediate in the uptake of methionine by this transport system.

Keywords: ABC transporter; methionine-binding protein; methionine transporter; MetNI, MetQ; L-methionine; transinhibition
Corresponding author: Douglas C. Rees, Division of Chemistry and Chemical Engineering 114-96, California Institute of Technology, Pasadena, CA 91125, USA; and Howard Hughes Medical Institute 114-96, California Institute of Technology, Pasadena, CA 91125, USA, e-mail:
aPresent address: California Institute for Quantitative Biosciences (QB3), MC2522, San Francisco, CA 94158, USA

Acknowledgments

A Vietnam International Education Development scholarship from the Vietnam Ministry of Education and Training scholarship to P.T.N, an NSF Graduate Fellowship to Q.W.L., and support of NIH Predoctoral Training Grant T32 GM07737 to N.S.K., are gratefully acknowledged. We thank Allen Lee for generating the original MetNIQ constructs, Christoph Müller for MetNIQ discussions, and Dr. Jens Kaiser and Dr. Nathan Dalleska for assistance with crystallography and ICP-MS, respectively. We gratefully acknowledge the Gordon and Betty Moore Foundation and the Beckman Institute for their generous support of the Molecular Observatory at Caltech and the staff at Beamline 12–2, Stanford Synchrotron Radiation Lightsource (SSRL), for their assistance with data collection. Use of the SSRL, SLAC National Accelerator Laboratory, is supported by the U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences under Contract No. DE-AC02-76SF00515. The SSRL Structural Molecular Biology Program is supported by the DOE Office of Biological and Environmental Research, and by the National Institutes of Health, National Institute of General Medical Sciences (including P41GM103393). This project benefited from the use of instrumentation made available by the Caltech Environmental Analysis Center. This work was supported in part by NIH grant GM045162.

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Received: 2015-2-18
Accepted: 2015-3-19
Published Online: 2015-3-23
Published in Print: 2015-9-1

©2015 by De Gruyter

Artikel in diesem Heft

  1. Frontmatter
  2. Meeting Report
  3. Membrane Transport and Communication in Frankfurt: Speakers’ Summary – Highlights
  4. HIGHLIGHT: MEMBRANE TRANSPORT AND COMMUNICATION
  5. Structure, function, evolution, and application of bacterial Pnu-type vitamin transporters
  6. Team work at its best – TAPL and its two domains
  7. The volume-regulated anion channel is formed by LRRC8 heteromers – molecular identification and roles in membrane transport and physiology
  8. Extending native mass spectrometry approaches to integral membrane proteins
  9. Functional diversity of the superfamily of K+ transporters to meet various requirements
  10. The structure of Na+-translocating of NADH:ubiquinone oxidoreductase of Vibrio cholerae: implications on coupling between electron transfer and Na+ transport
  11. Hybrid rotors in F1Fo ATP synthases: subunit composition, distribution, and physiological significance
  12. Homeostatic control of biological membranes by dedicated lipid and membrane packing sensors
  13. The transporter associated with antigen processing: a key player in adaptive immunity
  14. The pseudo-atomic structure of an RND-type tripartite multidrug efflux pump
  15. The assembly and disassembly of the AcrAB-TolC three-component multidrug efflux pump
  16. A universal mechanism for transport and regulation of CPA sodium proton exchangers
  17. Biosynthesis of membrane dependent proteins in insect cell lysates: identification of limiting parameters for folding and processing
  18. Fluorescence and excited state dynamics of the deprotonated Schiff base retinal in proteorhodopsin
  19. Regulatory role of charged clusters in the N-terminal domain of BetP from Corynebacterium glutamicum
  20. The contribution of methionine to the stability of the Escherichia coli MetNIQ ABC transporter-substrate binding protein complex
  21. The ABC exporter MsbA probed by solid state NMR – challenges and opportunities
  22. Functional properties of LptA and LptD in Anabaena sp. PCC 7120
https://doi.org/10.1515/hsz-2015-0131
Schlagwörter für diesen Artikel
ABC transporter; methionine-binding protein; methionine transporter; MetNI, MetQ; L-methionine; transinhibition

Artikel in diesem Heft

  1. Frontmatter
  2. Meeting Report
  3. Membrane Transport and Communication in Frankfurt: Speakers’ Summary – Highlights
  4. HIGHLIGHT: MEMBRANE TRANSPORT AND COMMUNICATION
  5. Structure, function, evolution, and application of bacterial Pnu-type vitamin transporters
  6. Team work at its best – TAPL and its two domains
  7. The volume-regulated anion channel is formed by LRRC8 heteromers – molecular identification and roles in membrane transport and physiology
  8. Extending native mass spectrometry approaches to integral membrane proteins
  9. Functional diversity of the superfamily of K+ transporters to meet various requirements
  10. The structure of Na+-translocating of NADH:ubiquinone oxidoreductase of Vibrio cholerae: implications on coupling between electron transfer and Na+ transport
  11. Hybrid rotors in F1Fo ATP synthases: subunit composition, distribution, and physiological significance
  12. Homeostatic control of biological membranes by dedicated lipid and membrane packing sensors
  13. The transporter associated with antigen processing: a key player in adaptive immunity
  14. The pseudo-atomic structure of an RND-type tripartite multidrug efflux pump
  15. The assembly and disassembly of the AcrAB-TolC three-component multidrug efflux pump
  16. A universal mechanism for transport and regulation of CPA sodium proton exchangers
  17. Biosynthesis of membrane dependent proteins in insect cell lysates: identification of limiting parameters for folding and processing
  18. Fluorescence and excited state dynamics of the deprotonated Schiff base retinal in proteorhodopsin
  19. Regulatory role of charged clusters in the N-terminal domain of BetP from Corynebacterium glutamicum
  20. The contribution of methionine to the stability of the Escherichia coli MetNIQ ABC transporter-substrate binding protein complex
  21. The ABC exporter MsbA probed by solid state NMR – challenges and opportunities
  22. Functional properties of LptA and LptD in Anabaena sp. PCC 7120
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