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Pyridine nucleotide complexes with Bacillus anthracis coenzyme A-disulfide reductase: a structural analysis of dual NAD(P)H specificity.

Wallen JR, Paige C, Mallett TC, Karplus PA, Claiborne A
Biochemistry 47 5182-93 (2008)
Related entries: 3cgb, 3cgc, 3cge

Cited: 22 times
EuropePMC logo PMID: 18399646

Abstract

We have recently reported that CoASH is the major low-molecular weight thiol in Bacillus anthracis [Nicely, N. I. , Parsonage, D., Paige, C., Newton, G. L., Fahey, R. C., Leonardi, R., Jackowski, S., Mallett, T. C., and Claiborne, A. (2007) Biochemistry 46, 3234-3245], and we have now characterized the kinetic and redox properties of the B. anthracis coenzyme A-disulfide reductase (CoADR, BACoADR) and determined the crystal structure at 2.30 A resolution. While the Staphylococcus aureus and Borrelia burgdorferi CoADRs exhibit strong preferences for NADPH and NADH, respectively, B. anthracis CoADR can use either pyridine nucleotide equally well. Sequence elements within the respective NAD(P)H-binding motifs correctly reflect the preferences for S. aureus and Bo. burgdorferi CoADRs, but leave questions as to how BACoADR can interact with both pyridine nucleotides. The structures of the NADH and NADPH complexes at ca. 2.3 A resolution reveal that a loop consisting of residues Glu180-Thr187 becomes ordered and changes conformation on NAD(P)H binding. NADH and NADPH interact with nearly identical conformations of this loop; the latter interaction, however, involves a novel binding mode in which the 2'-phosphate of NADPH points out toward solvent. In addition, the NAD(P)H-reduced BACoADR structures provide the first view of the reduced form (Cys42-SH/CoASH) of the Cys42-SSCoA redox center. The Cys42-SH side chain adopts a new conformation in which the conserved Tyr367'-OH and Tyr425'-OH interact with the nascent thiol(ate) on the flavin si-face. Kinetic data with Y367F, Y425F, and Y367,425F BACoADR mutants indicate that Tyr425' is the primary proton donor in catalysis, with Tyr367' functioning as a cryptic alternate donor in the absence of Tyr425'.

Articles - 3cgd mentioned but not cited (4)

  1. An Ancient Fingerprint Indicates the Common Ancestry of Rossmann-Fold Enzymes Utilizing Different Ribose-Based Cofactors. Laurino P, Tóth-Petróczy Á, Meana-Pañeda R, Lin W, Truhlar DG, Tawfik DS. PLoS Biol 14 e1002396 (2016)
  2. The coenzyme A disulphide reductase of Borrelia burgdorferi is important for rapid growth throughout the enzootic cycle and essential for infection of the mammalian host. Eggers CH, Caimano MJ, Malizia RA, Kariu T, Cusack B, Desrosiers DC, Hazlett KR, Claiborne A, Pal U, Radolf JD. Mol Microbiol 82 679-697 (2011)
  3. Novel role of 4-hydroxy-2-nonenal in AIFm2-mediated mitochondrial stress signaling. Miriyala S, Thippakorn C, Chaiswing L, Xu Y, Noel T, Tovmasyan A, Batinic-Haberle I, Vander Kooi CW, Chi W, Latif AA, Panchatcharam M, Prachayasittikul V, Butterfield DA, Vore M, Moscow J, St Clair DK. Free Radic Biol Med 91 68-80 (2016)
  4. Pyridine nucleotide complexes with Bacillus anthracis coenzyme A-disulfide reductase: a structural analysis of dual NAD(P)H specificity. Wallen JR, Paige C, Mallett TC, Karplus PA, Claiborne A. Biochemistry 47 5182-5193 (2008)


Reviews citing this publication (3)

  1. Low-molecular-weight thiols in thiol-disulfide exchange. Van Laer K, Hamilton CJ, Messens J. Antioxid Redox Signal 18 1642-1653 (2013)
  2. Bacillithiol, a new player in bacterial redox homeostasis. Helmann JD. Antioxid Redox Signal 15 123-133 (2011)
  3. Redox and Thiols in Archaea. Rawat M, Maupin-Furlow JA. Antioxidants (Basel) 9 E381 (2020)

Articles citing this publication (15)

  1. Bacillithiol is an antioxidant thiol produced in Bacilli. Newton GL, Rawat M, La Clair JJ, Jothivasan VK, Budiarto T, Hamilton CJ, Claiborne A, Helmann JD, Fahey RC. Nat Chem Biol 5 625-627 (2009)
  2. A General Tool for Engineering the NAD/NADP Cofactor Preference of Oxidoreductases. Cahn JK, Werlang CA, Baumschlager A, Brinkmann-Chen S, Mayo SL, Arnold FH. ACS Synth Biol 6 326-333 (2017)
  3. Characterization of the N-acetyl-α-D-glucosaminyl l-malate synthase and deacetylase functions for bacillithiol biosynthesis in Bacillus anthracis . Parsonage D, Newton GL, Holder RC, Wallace BD, Paige C, Hamilton CJ, Dos Santos PC, Redinbo MR, Reid SD, Claiborne A. Biochemistry 49 8398-8414 (2010)
  4. Anchored design of protein-protein interfaces. Lewis SM, Kuhlman BA. PLoS One 6 e20872 (2011)
  5. A genetically encoded tool for manipulation of NADP+/NADPH in living cells. Cracan V, Titov DV, Shen H, Grabarek Z, Mootha VK. Nat Chem Biol 13 1088-1095 (2017)
  6. Hydrogen Sulfide Sensing through Reactive Sulfur Species (RSS) and Nitroxyl (HNO) in Enterococcus faecalis. Shen J, Walsh BJC, Flores-Mireles AL, Peng H, Zhang Y, Zhang Y, Trinidad JC, Hultgren SJ, Giedroc DP. ACS Chem Biol 13 1610-1620 (2018)
  7. Crystal structure and catalytic properties of Bacillus anthracis CoADR-RHD: implications for flavin-linked sulfur trafficking. Wallen JR, Mallett TC, Boles W, Parsonage D, Furdui CM, Karplus PA, Claiborne A. Biochemistry 48 9650-9667 (2009)
  8. Cofactor Specificity Engineering of Streptococcus mutans NADH Oxidase 2 for NAD(P)(+) Regeneration in Biocatalytic Oxidations. Petschacher B, Staunig N, Müller M, Schürmann M, Mink D, De Wildeman S, Gruber K, Glieder A. Comput Struct Biotechnol J 9 e201402005 (2014)
  9. Cofactor specificity motifs and the induced fit mechanism in class I ketol-acid reductoisomerases. Cahn JK, Brinkmann-Chen S, Spatzal T, Wiig JA, Buller AR, Einsle O, Hu Y, Ribbe MW, Arnold FH. Biochem J 468 475-484 (2015)
  10. The type III pantothenate kinase encoded by coaX is essential for growth of Bacillus anthracis. Paige C, Reid SD, Hanna PC, Claiborne A. J Bacteriol 190 6271-6275 (2008)
  11. Analysis of disulphide bond linkage between CoA and protein cysteine thiols during sporulation and in spores of Bacillus species. Zhyvoloup A, Yu BYK, Baković J, Davis-Lunn M, Tossounian MA, Thomas N, Tsuchiya Y, Peak-Chew SY, Wigneshweraraj S, Filonenko V, Skehel M, Setlow P, Gout I. FEMS Microbiol Lett 367 fnaa174 (2020)
  12. Crystal structure of NADH:rubredoxin oxidoreductase from Clostridium acetobutylicum: a key component of the dioxygen scavenging system in obligatory anaerobes. Nishikawa K, Shomura Y, Kawasaki S, Niimura Y, Higuchi Y. Proteins 78 1066-1070 (2010)
  13. A broader active site in Pyrococcus horikoshii CoA disulfide reductase accommodates larger substrates and reveals evidence of subunit asymmetry. Sea K, Lee J, To D, Chen B, Sazinsky MH, Crane EJ. FEBS Open Bio 8 1083-1092 (2018)
  14. Turnover-dependent covalent inactivation of Staphylococcus aureus coenzyme A-disulfide reductase by coenzyme A-mimetics: mechanistic and structural insights. Wallace BD, Edwards JS, Wallen JR, Moolman WJ, van der Westhuyzen R, Strauss E, Redinbo MR, Claiborne A. Biochemistry 51 7699-7711 (2012)
  15. Structural and Kinetic Characterization of Hyperthermophilic NADH-Dependent Persulfide Reductase from Archaeoglobus fulgidus. Shabdar S, Anaclet B, Castineiras AG, Desir N, Choe N, Crane EJ, Sazinsky MH. Archaea 2021 8817136 (2021)


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