메뉴 건너뛰기




Volumn 46, Issue 13, 2007, Pages 3942-3951

3′-phosphoadenosine-5′-phosphosulfate reductase in complex with thioredoxin: A structural snapshot in the catalytic cycle

Author keywords

[No Author keywords available]

Indexed keywords

CATALYTIC CYCLE; CONFORMATIONAL CHANGES; DISULFIDES; GLUTATHIONE;

EID: 34047204205     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700130e     Document Type: Article
Times cited : (49)

References (48)
  • 2
    • 0028121632 scopus 로고
    • Photosynthetic Sulphate Reduction
    • Schwenn, J. D. (1994) Photosynthetic Sulphate Reduction, Z. Naturforsch. 49c, 531-539.
    • (1994) Z. Naturforsch , vol.49 c , pp. 531-539
    • Schwenn, J.D.1
  • 5
    • 0033988199 scopus 로고    scopus 로고
    • Identification of a new class of 5′-adenylylsulfate (APS) reductases from sulfate-assimilating bacteria
    • Bick, J. A., Dennis, J. J., Zylstra, G. J., Nowack, J., and Leustek, T. (2000) Identification of a new class of 5′-adenylylsulfate (APS) reductases from sulfate-assimilating bacteria, J. Bacteriol. 182, 135-142.
    • (2000) J. Bacteriol , vol.182 , pp. 135-142
    • Bick, J.A.1    Dennis, J.J.2    Zylstra, G.J.3    Nowack, J.4    Leustek, T.5
  • 6
    • 0028849610 scopus 로고
    • Reaction mechanism of thioredoxin: 3′-Phospho-adenylylsulfate reductase investigated by site-directed mutagenesis
    • Berendt, U., Haverkamp, T., Prior, A., and Schwenn, J. D. (1995) Reaction mechanism of thioredoxin: 3′-Phospho-adenylylsulfate reductase investigated by site-directed mutagenesis, Eur. J. Biochem. 233, 347-356.
    • (1995) Eur. J. Biochem , vol.233 , pp. 347-356
    • Berendt, U.1    Haverkamp, T.2    Prior, A.3    Schwenn, J.D.4
  • 7
    • 0024249959 scopus 로고
    • Yeast PAPS reductase: Properties and requirements of the purified enzyme
    • Schwenn, J. D., Krone, F. A., and Husmann, K. (1988) Yeast PAPS reductase: Properties and requirements of the purified enzyme, Arch. Microbiol. 150, 313-319.
    • (1988) Arch. Microbiol , vol.150 , pp. 313-319
    • Schwenn, J.D.1    Krone, F.A.2    Husmann, K.3
  • 8
    • 33750432874 scopus 로고    scopus 로고
    • Substrate recognition, protein dynamics, and iron-sulfur cluster in Pseudomonas aeruginosa adenosine 5′-phosphosulfate reductase
    • Chartron, J., Carroll, K. S., Shiau, C., Gao, H., Leary, J. A., Bertozzi, C. R., and Stout, C. D. (2006) Substrate recognition, protein dynamics, and iron-sulfur cluster in Pseudomonas aeruginosa adenosine 5′-phosphosulfate reductase, J. Mol. Biol. 364, 152-169.
    • (2006) J. Mol. Biol , vol.364 , pp. 152-169
    • Chartron, J.1    Carroll, K.S.2    Shiau, C.3    Gao, H.4    Leary, J.A.5    Bertozzi, C.R.6    Stout, C.D.7
  • 9
    • 0031571084 scopus 로고    scopus 로고
    • Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: A new family of adenine nucleotide α hydrolases
    • Savage, H., Montoya, G., Svensson, C., Schwenn, J. D., and Sinning, I. (1997) Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: A new family of adenine nucleotide α hydrolases, Structure 5, 895-906.
    • (1997) Structure , vol.5 , pp. 895-906
    • Savage, H.1    Montoya, G.2    Svensson, C.3    Schwenn, J.D.4    Sinning, I.5
  • 11
    • 0030766237 scopus 로고    scopus 로고
    • Trends in drug-resistant tuberculosis in the United States, 1993-1996
    • Moore, M., Onorato, I. M., McCray, E., and Castro, K. G. (1997) Trends in drug-resistant tuberculosis in the United States, 1993-1996, J. Am. Med. Assoc. 278, 833-837.
    • (1997) J. Am. Med. Assoc , vol.278 , pp. 833-837
    • Moore, M.1    Onorato, I.M.2    McCray, E.3    Castro, K.G.4
  • 12
    • 13844319812 scopus 로고    scopus 로고
    • The magic bullets and tuberculosis drug targets
    • Zhang, Y. (2005) The magic bullets and tuberculosis drug targets, Annu. Rev. Pharmacol. Toxicol. 45, 529-564.
    • (2005) Annu. Rev. Pharmacol. Toxicol , vol.45 , pp. 529-564
    • Zhang, Y.1
  • 13
    • 32444448306 scopus 로고    scopus 로고
    • Zhang, Y., Post-Martens, K., and Denkin, S. (2006) New drug candidates and therapeutic targets for tuberculosis therapy, Drug Discovery Today 11, 21-27.
    • Zhang, Y., Post-Martens, K., and Denkin, S. (2006) New drug candidates and therapeutic targets for tuberculosis therapy, Drug Discovery Today 11, 21-27.
  • 14
    • 0037031483 scopus 로고    scopus 로고
    • 5′-Adenosinephosphosulfate lies at a metabolic branch point in mycobacteria
    • Williams, S. J., Senaratne, R. H., Mougous, J. D., Riley, L. W., and Bertozzi, C. R. (2002) 5′-Adenosinephosphosulfate lies at a metabolic branch point in mycobacteria, J. Biol. Chem. 277, 32606-32615.
    • (2002) J. Biol. Chem , vol.277 , pp. 32606-32615
    • Williams, S.J.1    Senaratne, R.H.2    Mougous, J.D.3    Riley, L.W.4    Bertozzi, C.R.5
  • 15
    • 0036431696 scopus 로고    scopus 로고
    • Mycothiol biochemistry
    • Newton, G. L., and Fahey, R. C. (2002) Mycothiol biochemistry, Arch. Microbiol. 178, 388-394.
    • (2002) Arch. Microbiol , vol.178 , pp. 388-394
    • Newton, G.L.1    Fahey, R.C.2
  • 16
    • 0035940515 scopus 로고    scopus 로고
    • Comprehensive identification of conditionally essential genes in mycobacteria
    • Sassetti, C. M., Boyd, D. H., and Rubin, E. J. (2001) Comprehensive identification of conditionally essential genes in mycobacteria, Proc. Natl. Acad. Sci. U.S.A. 98, 12712-12717.
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 12712-12717
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 18
    • 0014939566 scopus 로고
    • The involvement of the thioredoxin system in the reduction of methionine sulfoxide and sulfate
    • Gonzalez Porque, P., Baldesten, A., and Reichard, P. (1970) The involvement of the thioredoxin system in the reduction of methionine sulfoxide and sulfate, J. Biol. Chem. 245, 2371-2374.
    • (1970) J. Biol. Chem , vol.245 , pp. 2371-2374
    • Gonzalez Porque, P.1    Baldesten, A.2    Reichard, P.3
  • 19
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • Holmgren, A. (1989) Thioredoxin and glutaredoxin systems, J. Biol. Chem. 264, 13963-13966.
    • (1989) J. Biol. Chem , vol.264 , pp. 13963-13966
    • Holmgren, A.1
  • 20
    • 0029165589 scopus 로고
    • Thioredoxin: A fold for all reasons
    • Martin, J. L. (1995) Thioredoxin: A fold for all reasons, Structure 3, 245-250.
    • (1995) Structure , vol.3 , pp. 245-250
    • Martin, J.L.1
  • 21
    • 33846419105 scopus 로고    scopus 로고
    • Noncovalent complexes of APS reductase from M. tuberculosis: Delineating a mechanistic model using ESI-FTICR MS
    • Gao, H., Leary, J., Carroll, K. S., Bertozzi, C. R., and Chen, H. (2007) Noncovalent complexes of APS reductase from M. tuberculosis: Delineating a mechanistic model using ESI-FTICR MS, J. Am. Soc. Mass Spectrom. 18, 167-178.
    • (2007) J. Am. Soc. Mass Spectrom , vol.18 , pp. 167-178
    • Gao, H.1    Leary, J.2    Carroll, K.S.3    Bertozzi, C.R.4    Chen, H.5
  • 22
    • 0033921672 scopus 로고    scopus 로고
    • Sulfate assimilation in higher plants: Characterization of a stable intermediate in the adenosine 5′-phosphosulfate reductase reaction
    • Weber, M., Suter, M., Brunold, C., and Kopriva, S. (2000) Sulfate assimilation in higher plants: Characterization of a stable intermediate in the adenosine 5′-phosphosulfate reductase reaction, Eur. J. Biochem. 267, 3647-3653.
    • (2000) Eur. J. Biochem , vol.267 , pp. 3647-3653
    • Weber, M.1    Suter, M.2    Brunold, C.3    Kopriva, S.4
  • 23
    • 0014006918 scopus 로고
    • Thioredoxin from Lactobacillus leichmannii and its role as hydrogen donor for ribonucleoside triphosphate reductase
    • Orr, M. D., and Vitols, E. (1966) Thioredoxin from Lactobacillus leichmannii and its role as hydrogen donor for ribonucleoside triphosphate reductase, Biochem. Biophys. Res. Commun. 25, 109-115.
    • (1966) Biochem. Biophys. Res. Commun , vol.25 , pp. 109-115
    • Orr, M.D.1    Vitols, E.2
  • 24
    • 0034680847 scopus 로고    scopus 로고
    • A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli
    • Boschi-Muller, S., Azza, S., Sanglier-Cianferani, S., Talfournier, F., Van Dorsselear, A., and Branlant, G. (2000) A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli, J. Biol. Chem. 275, 35908-35913.
    • (2000) J. Biol. Chem , vol.275 , pp. 35908-35913
    • Boschi-Muller, S.1    Azza, S.2    Sanglier-Cianferani, S.3    Talfournier, F.4    Van Dorsselear, A.5    Branlant, G.6
  • 25
    • 33846393586 scopus 로고    scopus 로고
    • Structural basis for target protein recognition by the protein disulfide reductase thioredoxin
    • Maeda, K., Hagglund, P., Finnie, C., Svensson, B., and Henriksen, A. (2006) Structural basis for target protein recognition by the protein disulfide reductase thioredoxin, Structure 14, 1701-1710.
    • (2006) Structure , vol.14 , pp. 1701-1710
    • Maeda, K.1    Hagglund, P.2    Finnie, C.3    Svensson, B.4    Henriksen, A.5
  • 28
    • 0028103275 scopus 로고    scopus 로고
    • Collaborative Computational Project No. 4 (1994) The CCP4 suite: Programs for protein crystallography, Acta Crystallogr. D50, 760-763.
    • Collaborative Computational Project No. 4 (1994) The CCP4 suite: Programs for protein crystallography, Acta Crystallogr. D50, 760-763.
  • 29
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method, Acta Crystallogr. D53, 240-255.
    • (1997) Acta Crystallogr , vol.D53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 30
    • 14844321328 scopus 로고    scopus 로고
    • Refinement of severely incomplete structures with maximum likelihood in BUSTER-TNT
    • Blanc, E., Roversi, P., Vonrhein, C., Flensburg, C., Lea, S. M., and Bricogne, G. (2004) Refinement of severely incomplete structures with maximum likelihood in BUSTER-TNT, Acta Crystallogr. D60, 2210-2221.
    • (2004) Acta Crystallogr , vol.D60 , pp. 2210-2221
    • Blanc, E.1    Roversi, P.2    Vonrhein, C.3    Flensburg, C.4    Lea, S.M.5    Bricogne, G.6
  • 31
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit: A versatile program for manipulating atomic coordinates and electron density
    • McRee, D. E. (1999) XtalView/Xfit: A versatile program for manipulating atomic coordinates and electron density, J. Struct. Biol. 125, 156-165.
    • (1999) J. Struct. Biol , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 34
    • 0032532240 scopus 로고    scopus 로고
    • NMR characterization of a single-cysteine mutant of Escherichia coli thioredoxin and a covalent thioredoxin-peptide complex
    • Jeng, M. F., Reymond, M. T., Tennant, L. L., Holmgren, A., and Dyson, H. J. (1998) NMR characterization of a single-cysteine mutant of Escherichia coli thioredoxin and a covalent thioredoxin-peptide complex, Eur. J. Biochem. 257, 299-308.
    • (1998) Eur. J. Biochem , vol.257 , pp. 299-308
    • Jeng, M.F.1    Reymond, M.T.2    Tennant, L.L.3    Holmgren, A.4    Dyson, H.J.5
  • 36
    • 0029070171 scopus 로고
    • Omega loops: Nonregular secondary structures significant in protein function and stability
    • Fetrow, J. S. (1995) Omega loops: Nonregular secondary structures significant in protein function and stability, FASEB J. 9, 708-717.
    • (1995) FASEB J , vol.9 , pp. 708-717
    • Fetrow, J.S.1
  • 37
    • 33745161382 scopus 로고    scopus 로고
    • Allosteric disulfide bonds
    • Schmidt, B., Ho, L., and Hogg, P. J. (2006) Allosteric disulfide bonds, Biochemistry 45, 7429-7433.
    • (2006) Biochemistry , vol.45 , pp. 7429-7433
    • Schmidt, B.1    Ho, L.2    Hogg, P.J.3
  • 38
  • 39
    • 0033582607 scopus 로고    scopus 로고
    • NMR structure of Escherichia coli glutaredoxin 3-glutathione mixed disulfide complex: Implications for the enzymatic mechanism
    • Nordstrand, K., Åslund, F., Holmgren, Å., Otting, G., and Berndt, K. D. (1999) NMR structure of Escherichia coli glutaredoxin 3-glutathione mixed disulfide complex: Implications for the enzymatic mechanism, J. Mol. Biol. 286, 541-552.
    • (1999) J. Mol. Biol , vol.286 , pp. 541-552
    • Nordstrand, K.1    Åslund, F.2    Holmgren, A.3    Otting, G.4    Berndt, K.D.5
  • 40
    • 0033543666 scopus 로고    scopus 로고
    • Binding specificity and mechanistic insight into glutaredoxin-catalyzed protein disulfide reduction
    • Berardi, M. J., and Bushweller, J. H. (1999) Binding specificity and mechanistic insight into glutaredoxin-catalyzed protein disulfide reduction, J. Mol. Biol. 292, 151-161.
    • (1999) J. Mol. Biol , vol.292 , pp. 151-161
    • Berardi, M.J.1    Bushweller, J.H.2
  • 41
    • 0028181442 scopus 로고
    • The nuclear magnetic resonance solution structure of the mixed disulfide between Escherichia coli glutaredoxin(C14S) and glutathione
    • Bushweller, J. H., Billeter, M., Holmgren, A., and Wuthrich, K. (1994) The nuclear magnetic resonance solution structure of the mixed disulfide between Escherichia coli glutaredoxin(C14S) and glutathione, J. Mol. Biol. 235, 1585-1597.
    • (1994) J. Mol. Biol , vol.235 , pp. 1585-1597
    • Bushweller, J.H.1    Billeter, M.2    Holmgren, A.3    Wuthrich, K.4
  • 42
    • 27744499033 scopus 로고    scopus 로고
    • Mechanisms of iron-sulfur cluster assembly: The SUF machinery
    • Fontecave, M., Choudens, S. O., Py, B., and Barras, F. (2005) Mechanisms of iron-sulfur cluster assembly: The SUF machinery, J. Biol. Inorg. Chem. 10, 713-721.
    • (2005) J. Biol. Inorg. Chem , vol.10 , pp. 713-721
    • Fontecave, M.1    Choudens, S.O.2    Py, B.3    Barras, F.4
  • 43
    • 0037047411 scopus 로고    scopus 로고
    • A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids
    • Takahashi, Y., and Tokumoto, U. (2002) A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids, J. Biol. Chem. 277, 28380-28383.
    • (2002) J. Biol. Chem , vol.277 , pp. 28380-28383
    • Takahashi, Y.1    Tokumoto, U.2
  • 44
    • 0028265941 scopus 로고
    • Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene product
    • Zheng, L., White, R. H., Cash, V. L., and Dean, D. R. (1994) Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene product, Biochemistry 33, 4714-4720.
    • (1994) Biochemistry , vol.33 , pp. 4714-4720
    • Zheng, L.1    White, R.H.2    Cash, V.L.3    Dean, D.R.4
  • 45
    • 0345303679 scopus 로고    scopus 로고
    • Mechanistic studies of the SufS-SufE cysteine desulfurase: Evidence for sulfur transfer from SufS to SufE
    • Ollagnier-de-Choudens, S., Lascoux, D., Loiseau, L., Barras, F., Forest, E., and Fontecave, M. (2003) Mechanistic studies of the SufS-SufE cysteine desulfurase: Evidence for sulfur transfer from SufS to SufE, FEBS Lett. 555, 263-267.
    • (2003) FEBS Lett , vol.555 , pp. 263-267
    • Ollagnier-de-Choudens, S.1    Lascoux, D.2    Loiseau, L.3    Barras, F.4    Forest, E.5    Fontecave, M.6
  • 46
    • 4644275046 scopus 로고    scopus 로고
    • Kinetic and structural characterization of Slr0077/SufS, the essential cysteine desulfurase from Synechocystis sp. PCC 6803
    • Tirupati, B., Vey, J. L., Drennan, C. L., and Bollinger, J. M., Jr. (2004) Kinetic and structural characterization of Slr0077/SufS, the essential cysteine desulfurase from Synechocystis sp. PCC 6803, Biochemistry 43, 12210-12219.
    • (2004) Biochemistry , vol.43 , pp. 12210-12219
    • Tirupati, B.1    Vey, J.L.2    Drennan, C.L.3    Bollinger Jr., J.M.4
  • 47
    • 0034682854 scopus 로고    scopus 로고
    • Twists in catalysis: Alternating conformations of Escherichia coli thioredoxin reductase
    • Lennon, B. W., Williams, C. H., Jr., and Ludwig, M. L. (2000) Twists in catalysis: Alternating conformations of Escherichia coli thioredoxin reductase, Science 289, 1190-1194.
    • (2000) Science , vol.289 , pp. 1190-1194
    • Lennon, B.W.1    Williams Jr., C.H.2    Ludwig, M.L.3
  • 48
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 22 Å resolution
    • Doublie, S., Tabor, S., Long, A. M., Richardson, C. C., and Ellenberger, T. (1998) Crystal structure of a bacteriophage T7 DNA replication complex at 22 Å resolution, Nature 391, 251-258.
    • (1998) Nature , vol.391 , pp. 251-258
    • Doublie, S.1    Tabor, S.2    Long, A.M.3    Richardson, C.C.4    Ellenberger, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.