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NrdH-redoxin of Mycobacterium tuberculosis and Corynebacterium glutamicum dimerizes at high protein concentration and exclusively receives electrons from thioredoxin reductase.

Bibliographic reference Van Laer, K ; Dziewulska, A.M. ; Fislage, M. ; Hbeddou, A. ; Wahni, K. ; et. al. NrdH-redoxin of Mycobacterium tuberculosis and Corynebacterium glutamicum dimerizes at high protein concentration and exclusively receives electrons from thioredoxin reductase.. In: Journal of Biological Chemistry, Vol. 288, no. 11, p. 7942-55 (2013)
Permanent URL http://hdl.handle.net/2078.1/120318
  1. Lundin Daniel, Torrents Eduard, Poole Anthony M, Sjöberg Britt-Marie, RNRdb, a curated database of the universal enzyme family ribonucleotide reductase, reveals a high level of misannotation in sequences deposited to Genbank, 10.1186/1471-2164-10-589
  2. Jordan Albert, Åslund Fredrik, Pontis Elisabet, Reichard Peter, Holmgren Arne, Characterization ofEscherichia coliNrdH : A GLUTAREDOXIN-LIKE PROTEIN WITH A THIOREDOXIN-LIKE ACTIVITY PROFILE, 10.1074/jbc.272.29.18044
  3. Rabinovitch I., Yanku M., Yeheskel A., Cohen G., Borovok I., Aharonowitz Y., Staphylococcus aureus NrdH Redoxin Is a Reductant of the Class Ib Ribonucleotide Reductase, 10.1128/jb.00539-10
  4. Boal A. K., Cotruvo J. A., Stubbe J., Rosenzweig A. C., Structural Basis for Activation of Class Ib Ribonucleotide Reductase, 10.1126/science.1190187
  5. Van Laer Koen, Hamilton Chris J., Messens Joris, Low-Molecular-Weight Thiols in Thiol–Disulfide Exchange, 10.1089/ars.2012.4964
  6. Newton Gerald L, Rawat Mamta, La Clair James J, Jothivasan Vishnu Karthik, Budiarto Tanya, Hamilton Chris J, Claiborne Al, Helmann John D, Fahey Robert C, Bacillithiol is an antioxidant thiol produced in Bacilli, 10.1038/nchembio.189
  7. Gustafsson Tomas N., Sahlin Margareta, Lu Jun, Sjöberg Britt-Marie, Holmgren Arne, Bacillus anthracisThioredoxin Systems, Characterization and Role as Electron Donors for Ribonucleotide Reductase, 10.1074/jbc.m112.413427
  8. Ordóñez Efrén, Van Belle Karolien, Roos Goedele, De Galan Sandra, Letek Michal, Gil Jose A., Wyns Lode, Mateos Luis M., Messens Joris, Arsenate Reductase, Mycothiol, and Mycoredoxin Concert Thiol/Disulfide Exchange, 10.1074/jbc.m900877200
  9. Van Laer Koen, Buts Lieven, Foloppe Nicolas, Vertommen Didier, Van Belle Karolien, Wahni Khadija, Roos Goedele, Nilsson Lennart, Mateos Luis M., Rawat Mamta, van Nuland Nico A. J., Messens Joris, Mycoredoxin-1 is one of the missing links in the oxidative stress defence mechanism of Mycobacteria : Mycoredoxin-1 links mycothiol to oxidative stress, 10.1111/mmi.12030
  10. Roos Goedele, Garcia-Pino Abel, Van belle Karolien, Brosens Elke, Wahni Khadija, Vandenbussche Guy, Wyns Lode, Loris Remy, Messens Joris, The Conserved Active Site Proline Determines the Reducing Power of Staphylococcus aureus Thioredoxin, 10.1016/j.jmb.2007.02.045
  11. Kabsch W., Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector, 10.1107/s0021889888007903
  12. Long Fei, Vagin Alexei A., Young Paul, Murshudov Garib N., BALBES: a molecular-replacement pipeline, 10.1107/s0907444907050172
  13. Nordlund Pär, Reichard Peter, Ribonucleotide Reductases, 10.1146/annurev.biochem.75.103004.142443
  14. Stehr Matthias, Schneider Gunter, Åslund Fredrik, Holmgren Arne, Lindqvist Ylva, Structural Basis for the Thioredoxin-like Activity Profile of the Glutaredoxin-like NrdH-redoxin fromEscherichia coli, 10.1074/jbc.m105094200
  15. Eklund Hans, Ingelman Margareta, Söderberg Bengt-Olof, Uhlin Tomas, Nordlund Pär, Nikkola Matti, Sonnerstam Ulf, Joelson Thorleif, Petratos Kyriacos, Structure of oxidized bacteriophage T4 glutaredoxin (thioredoxin), 10.1016/0022-2836(92)90844-a
  16. Langer Gerrit, Cohen Serge X, Lamzin Victor S, Perrakis Anastassis, Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7, 10.1038/nprot.2008.91
  17. Emsley Paul, Cowtan Kevin, Coot: model-building tools for molecular graphics, 10.1107/s0907444904019158
  18. Adams Paul D., Afonine Pavel V., Bunkóczi Gábor, Chen Vincent B., Davis Ian W., Echols Nathaniel, Headd Jeffrey J., Hung Li-Wei, Kapral Gary J., Grosse-Kunstleve Ralf W., McCoy Airlie J., Moriarty Nigel W., Oeffner Robert, Read Randy J., Richardson David C., Richardson Jane S., Terwilliger Thomas C., Zwart Peter H., PHENIX: a comprehensive Python-based system for macromolecular structure solution, 10.1107/s0907444909052925
  19. Painter Jay, Merritt Ethan A., Optimal description of a protein structure in terms of multiple groups undergoing TLS motion, 10.1107/s0907444906005270
  20. Painter Jay, Merritt Ethan A., TLSMDweb server for the generation of multi-group TLS models, 10.1107/s0021889805038987
  21. Lassmann Timo, Sonnhammer ErikLL, 10.1186/1471-2105-6-298
  22. Eswar Narayanan, Webb Ben, Marti-Renom Marc A., Madhusudhan M.S., Eramian David, Shen Min-yi, Pieper Ursula, Sali Andrej, Comparative Protein Structure Modeling Using Modeller, 10.1002/0471250953.bi0506s15
  23. Eklund Hans, Uhlin Ulla, Färnegårdh Mathias, Logan Derek T., Nordlund Pär, Structure and function of the radical enzyme ribonucleotide reductase, 10.1016/s0079-6107(01)00014-1
  24. Lennon B. W., Twists in Catalysis: Alternating Conformations of Escherichia coli Thioredoxin Reductase, 10.1126/science.289.5482.1190
  25. Akif Mohd, Suhre Karsten, Verma Chandra, Mande Shekhar C., Conformational flexibility ofMycobacterium tuberculosisthioredoxin reductase: crystal structure and normal-mode analysis, 10.1107/s0907444905030519
  26. Hess Berk, Kutzner Carsten, van der Spoel David, Lindahl Erik, GROMACS 4:  Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation, 10.1021/ct700301q
  27. Dolinsky T. J., Nielsen J. E., McCammon J. A., Baker N. A., PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations, 10.1093/nar/gkh381
  28. Baker N. A., Sept D., Joseph S., Holst M. J., McCammon J. A., Electrostatics of nanosystems: Application to microtubules and the ribosome, 10.1073/pnas.181342398
  29. Larkin M.A., Blackshields G., Brown N.P., Chenna R., McGettigan P.A., McWilliam H., Valentin F., Wallace I.M., Wilm A., Lopez R., Thompson J.D., Gibson T.J., Higgins D.G., Clustal W and Clustal X version 2.0, 10.1093/bioinformatics/btm404
  30. Konarev Petr V., Volkov Vladimir V., Sokolova Anna V., Koch Michel H. J., Svergun Dmitri I., PRIMUS: a Windows PC-based system for small-angle scattering data analysis, 10.1107/s0021889803012779
  31. Guinier A. Fournet G. (1955) Small-angle Scattering of X-rays, John Wiley & Sons, Inc., New York
  32. Porod G. (1982) Small Angle X-ray Scattering, pp. 17–51, Academic Press, Inc., New York
  33. Svergun D. I., Determination of the regularization parameter in indirect-transform methods using perceptual criteria, 10.1107/s0021889892001663
  34. Reichard P, Ehrenberg A, Ribonucleotide reductase--a radical enzyme, 10.1126/science.6306767
  35. Konarev Petr V., Petoukhov Maxim V., Volkov Vladimir V., Svergun Dmitri I., ATSAS2.1, a program package for small-angle scattering data analysis, 10.1107/s0021889806004699
  36. Fernández-González C., Gil J. A., Mateos L. M., Schwarzer A., Schäfer A., Kalinowski J., Pühler A., Martín J. F., Construction of L-lysine-overproducing strains of Brevibacterium lactofermentum by targeted disruption of the hom and thrB genes, 10.1007/s002530050860
  37. Jäger W, Schäfer A, Pühler A, Labes G, Wohlleben W, Expression of the Bacillus subtilis sacB gene leads to sucrose sensitivity in the gram-positive bacterium Corynebacterium glutamicum but not in Streptomyces lividans., 10.1128/jb.174.16.5462-5465.1992
  38. Ordóñez Efrén, Thiyagarajan Saravanamuthu, Cook Jeremy D., Stemmler Timothy L., Gil José A., Mateos Luís M., Rosen Barry P., Evolution of Metal(loid) Binding Sites in Transcriptional Regulators, 10.1074/jbc.m803209200
  39. Patel Mehul P., Blanchard John S., Expression, Purification, and Characterization ofMycobacterium tuberculosisMycothione Reductase†, 10.1021/bi991025h
  40. Akif M., Khare G., Tyagi A. K., Mande S. C., Sardesai A. A., Functional Studies of Multiple Thioredoxins from Mycobacterium tuberculosis, 10.1128/jb.00159-08
  41. Garcia-Pino Abel, Martinez-Rodriguez Sergio, Wahni Khadija, Wyns Lode, Loris Remy, Messens Joris, Coupling of Domain Swapping to Kinetic Stability in a Thioredoxin Mutant, 10.1016/j.jmb.2008.11.040
  42. Rousseau Frederic, Schymkowitz Joost W.H., Itzhaki Laura S., The Unfolding Story of Three-Dimensional Domain Swapping, 10.1016/s0969-2126(03)00029-7
  43. Liu Yanshun, Eisenberg David, 3D domain swapping: As domains continue to swap, 10.1110/ps.0201402
  44. Newcomer Marcia E., 10.1038/86134
  45. NILSSON OLLE, LUNDQVIST TOMAS, HAHNE SOLVEIG, SJÖBERG BRITT-MARIE, Structure-function studies of the large subunit of ribonucleotide reductase fromEscherichia coli, 10.1042/bst0160091
  46. Kiefer F., Arnold K., Kunzli M., Bordoli L., Schwede T., The SWISS-MODEL Repository and associated resources, 10.1093/nar/gkn750
  47. Leiting W.U., Jianping X.I.E., Comparative genomics analysis of Mycobacterium NrdH-redoxins, 10.1016/j.micpath.2010.01.004
  48. Jensen Kristine Steen, Hansen Rosa E., Winther Jakob R., Kinetic and Thermodynamic Aspects of Cellular Thiol–Disulfide Redox Regulation, 10.1089/ars.2008.2297
  49. Roos Goedele, Foloppe Nicolas, Messens Joris, Understanding the pKaof Redox Cysteines: The Key Role of Hydrogen Bonding, 10.1089/ars.2012.4521
  50. Collet Jean-Francois, Messens Joris, Structure, Function, and Mechanism of Thioredoxin Proteins, 10.1089/ars.2010.3114
  51. Roos Goedele, Loverix Stefan, Geerlings Paul, Origin of the pKaPerturbation of N-Terminal Cysteine in α- and 310-Helices:  A Computational DFT Study, 10.1021/jp0549780
  52. Roos Goedele, Foloppe Nicolas, Van Laer Koen, Wyns Lode, Nilsson Lennart, Geerlings Paul, Messens Joris, How Thioredoxin Dissociates Its Mixed Disulfide, 10.1371/journal.pcbi.1000461
  53. Sassetti Christopher M., Boyd Dana H., Rubin Eric J., Genes required for mycobacterial growth defined by high density mutagenesis : Genes required for mycobacterial growth, 10.1046/j.1365-2958.2003.03425.x
  54. Harris Thomas K., Turner George J., Structural Basis of Perturbed pKa Values of Catalytic Groups in Enzyme Active Sites, 10.1080/15216540211468
  55. Williams Charles H., Arscott L. David, Müller Sylke, Lennon Brett W., Ludwig Martha L., Wang Pan-Fen, Veine Donna M., Becker Katja, Schirmer R. Heiner, Thioredoxin reductase : Two modes of catalysis have evolved, 10.1046/j.1432-1327.2000.01702.x
  56. Chebotareva, Biochemistry, 69, 1239 (2004)
  57. Jordan A., Pontis E., Atta M., Krook M., Gibert I., Barbe J., Reichard P., A second class I ribonucleotide reductase in Enterobacteriaceae: characterization of the Salmonella typhimurium enzyme., 10.1073/pnas.91.26.12892
  58. Mowa Mohube B., Warner Digby F., Kaplan Gilla, Kana Bavesh D., Mizrahi Valerie, Function and Regulation of Class I Ribonucleotide Reductase-Encoding Genes in Mycobacteria, 10.1128/jb.01409-08
  59. KOLBERG M, Structure, function, and mechanism of ribonucleotide reductases, 10.1016/s1570-9639(04)00054-8
  60. Stehr Matthias, Lindqvist Ylva, NrdH-redoxin of Corynebacterium ammoniagenes forms a domain-swapped dimer, 10.1002/prot.20126