Structure of a bacterial energy-coupling factor transporter

Nature

Volumn 497, Issue 7448, 2013, Pages 272-276

  Wang, Tingliang ^a   Fu, Guobin ^a   Pan, Xiaojing ^a   Wu, Jianping ^a   Gong, Xinqi ^a   Wang, Jiawei ^a   Shi, Yigong ^a  

^a TSINGHUA UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; ENERGY COUPLING FACTOR; MEMBRANE PROTEIN; PYRIMIDINE DERIVATIVE; UNCLASSIFIED DRUG;

BACTERIUM; CHEMICAL BINDING; CRYSTAL STRUCTURE; CYTOPLASM; LIPID; MEMBRANE; PROTEIN;

ALPHA HELIX; ARTICLE; BINDING AFFINITY; CRYSTAL STRUCTURE; CRYSTALLIZATION; CYTOSOL; DIMERIZATION; ENERGY TRANSFER; HYDROGEN BOND; LACTOBACILLUS BREVIS; LIPID MEMBRANE; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN HYDROLYSIS; PROTEIN STRUCTURE; PROTEIN TRANSPORT; STOICHIOMETRY;

ANTI-BACTERIAL AGENTS; ATP-BINDING CASSETTE TRANSPORTERS; BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; CYTOPLASM; LACTOBACILLUS BREVIS; MODELS, BIOLOGICAL; MODELS, MOLECULAR; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; PYRIMIDINES; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); LACTOBACILLUS BREVIS; PROKARYOTA;

EID: 84877766581     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature12045     Document Type: Article

References (32)

1. Rodionov, D. A. et al. A novel class of modular transporters for vitamins in prokaryotes. J. Bacteriol. 191, 42-51 (2009).
2. Eitinger, T., Rodionov, D. A., Grote, M. & Schneider, E. Canonical and ECF-type ATPbinding cassette importers in prokaryotes: diversity in modular organization and cellular functions. FEMS Microbiol. Rev. 35, 3-67 (2011).
3. Erkens, G. B., Majsnerowska, M., Ter Beek, J. & Slotboom, D. J. Energy coupling factor-type ABC transporters for vitamin uptake in prokaryotes. Biochemistry 51, 4390-4396 (2012).
4. Rees, D. C., Johnson, E. & Lewinson, O. ABC transporters: the power to change. Nature Rev. Mol. Cell Biol. 10, 218-227 (2009).
5. Oldham, M. L., Khare, D., Quiocho, F. A., Davidson, A. L. & Chen, J. Crystal structure of a catalytic intermediate of the maltose transporter. Nature 450, 515-521 (2007).
6. Oldham, M. L. & Chen, J. Crystal structure of the maltose transporter in a pretranslocation intermediate state. Science 332, 1202-1205 (2011).
7. Oldham, M. L. & Chen, J. Snapshots of the maltose transporter during ATP hydrolysis. Proc. Natl Acad. Sci. USA 108, 15152-15156 (2011).
8. Locher, K. P., Lee, A. T. & Rees, D. C. The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism. Science 296, 1091-1098 (2002).
9. Pinkett, H. W., Lee, A. T., Lum, P., Locher, K. P. & Rees, D. C. An inward-facing conformation of a putative metal-chelate-type ABC transporter. Science 315, 373-377 (2007).
10. Hvorup, R. N. et al. Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF. Science 317, 1387-1390 (2007).
11. Dawson, R. J. & Locher, K. P. Structure of a bacterial multidrug ABC transporter. Nature 443, 180-185 (2006).
12. Dawson, R. J. & Locher, K. P. Structure of the multidrug ABC transporter Sav1866 fromStaphylococcus aureus in complex withAMP-PNP. FEBS Lett. 581, 935-938 (2007).
13. Duurkens, R. H., Tol, M. B., Geertsma, E. R., Permentier, H. P. & Slotboom, D. J. Flavin binding to the high affinity riboflavin transporter RibU. J. Biol. Chem. 282, 10380-10386 (2007).
14. Hebbeln, P., Rodionov, D. A., Alfandega, A. & Eitinger, T. Biotin uptake in prokaryotes by solute transporters with an optional ATP-binding cassettecontaining module. Proc. Natl Acad. Sci. USA 104, 2909-2914 (2007).
15. Erkens, G. B. & Slotboom, D. J. Biochemical characterization of ThiT from Lactococcus lactis: a thiamin transporter with picomolar substrate binding affinity. Biochemistry 49, 3203-3212 (2010).
16. Zhang, P., Wang, J. & Shi, Y. Structure and mechanism of the S component of a bacterial ECF transporter. Nature 468, 717-720 (2010).
17. Erkens, G. B. et al. The structural basis ofmodularity in ECF-type ABC transporters. Nature Struct. Mol. Biol. 18, 755-760 (2011).
18. Berntsson, R. P. et al. Structural divergence of paralogous S components from ECF-type ABC transporters. Proc. Natl Acad. Sci. USA 109, 13990-13995 (2012).
19. Holm, L. & Sander, C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138 (1993).
20. Seyedarabi, A., Sullivan, J. A., Sasakawa, C. & Pickersgill, R. W. A disulfide driven domain swap switches off the activity of Shigella IpaH9.8 E3 ligase. FEBS Lett. 584, 4163-4168 (2010).
21. Neubauer, O. et al. Two essential arginine residues in the T components of energycoupling factor transporters. J. Bacteriol. 191, 6482-6488 (2009).
22. Lezon, T. R. & Bahar, I. Constraintsimposed by themembrane selectively guide the alternating access dynamics of the glutamate transporter GltPh. Biophys. J. 102, 1331-1340 (2012).
23. Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
24. Schneider, T. R. & Sheldrick, G. M. Substructure solution with SHELXD. Acta Crystallogr. D 58, 1772-1779 (2002).
25. McCoy, A. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007).
26. Cowtan, K. & DM: an automated procedure for phase improvement by density modification. CCP4 Newslett. 31, 34-38 (1994).
27. Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132 (2004).
28. DeLaBarre, B. & Brunger, A. T. Considerations for the refinement of low-resolution crystal structures. Acta Crystallogr. D 62, 923-932 (2006).
29. Adams, P. D. et al. PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr. D 58, 1948-1954 (2002).
30. DeLano, W. L. The PyMOL Molecular Graphics System. http://www.pymol.org (2002).
31. Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
32. Humphrey, W., Dalke, A. & Schulten, K. VMD: visual molecular dynamics. J. Mol. Graph. 14, 33-38 (1996).