메뉴 건너뛰기




Volumn 54, Issue 34, 2015, Pages 5322-5328

Hydrogen-Deuterium Exchange Mass Spectrometry Reveals Unique Conformational and Chemical Transformations Occurring upon [4Fe-4S] Cluster Binding in the Type 2 L-Serine Dehydratase from Legionella pneumophila

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CONFORMATIONS; COVALENT BONDS; CRYSTAL ATOMIC STRUCTURE; DEHYDRATION; DEUTERIUM; MASS SPECTROMETRY; PEPTIDES; PROTEINS; SPECTROMETRY;

EID: 84940762342     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.5b00761     Document Type: Article
Times cited : (9)

References (28)
  • 1
    • 33646368396 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Ever-expanding roles
    • Fontecave, M. (2006) Iron-sulfur clusters: ever-expanding roles Nat. Chem. Biol. 2, 171-174 10.1038/nchembio0406-171
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 171-174
    • Fontecave, M.1
  • 2
    • 77952813340 scopus 로고    scopus 로고
    • Building Fe-S proteins: Bacterial strategies
    • Py, B. and Barras, F. (2010) Building Fe-S proteins: bacterial strategies Nat. Rev. Microbiol. 8, 436-446 10.1038/nrmicro2356
    • (2010) Nat. Rev. Microbiol. , vol.8 , pp. 436-446
    • Py, B.1    Barras, F.2
  • 3
    • 84884901489 scopus 로고    scopus 로고
    • Iron/Sulfur proteins biogenesis in prokaryotes: Formation, regulation and diversity
    • Roche, B., Aussel, L., Ezraty, B., Mandin, P., Py, B., and Barras, F. (2013) Iron/Sulfur proteins biogenesis in prokaryotes: Formation, regulation and diversity Biochim. Biophys. Acta, Bioenerg. 1827, 923-937 10.1016/j.bbabio.2013.05.001
    • (2013) Biochim. Biophys. Acta, Bioenerg. , vol.1827 , pp. 923-937
    • Roche, B.1    Aussel, L.2    Ezraty, B.3    Mandin, P.4    Py, B.5    Barras, F.6
  • 4
    • 79954617423 scopus 로고    scopus 로고
    • Fe-S clusters, fragile sentinels of the cell
    • Py, B., Moreau, P. L., and Barras, F. (2011) Fe-S clusters, fragile sentinels of the cell Curr. Opin. Microbiol. 14, 218-223 10.1016/j.mib.2011.01.004
    • (2011) Curr. Opin. Microbiol. , vol.14 , pp. 218-223
    • Py, B.1    Moreau, P.L.2    Barras, F.3
  • 5
    • 0014024195 scopus 로고
    • The reconstitution of clostridial ferredoxin
    • Malkin, R. and Rabinowitz, J. C. (1966) The reconstitution of clostridial ferredoxin Biochem. Biophys. Res. Commun. 23, 822-827 10.1016/0006-291X(66)90561-4
    • (1966) Biochem. Biophys. Res. Commun. , vol.23 , pp. 822-827
    • Malkin, R.1    Rabinowitz, J.C.2
  • 6
    • 7244239273 scopus 로고    scopus 로고
    • Repair of oxidized iron-sulfur clusters in Escherichia coli
    • Djaman, O., Outten, F. W., and Imlay, J. A. (2004) Repair of oxidized iron-sulfur clusters in Escherichia coli J. Biol. Chem. 279, 44590-44599 10.1074/jbc.M406487200
    • (2004) J. Biol. Chem. , vol.279 , pp. 44590-44599
    • Djaman, O.1    Outten, F.W.2    Imlay, J.A.3
  • 7
    • 0001531847 scopus 로고    scopus 로고
    • Iron-Sulfur Proteins with Nonredox Functions
    • Flint, D. H. and Allen, R. M. (1996) Iron-Sulfur Proteins with Nonredox Functions Chem. Rev. 96, 2315-2334 10.1021/cr950041r
    • (1996) Chem. Rev. , vol.96 , pp. 2315-2334
    • Flint, D.H.1    Allen, R.M.2
  • 8
    • 0021112560 scopus 로고
    • Optical and EPR characterization of different species of active and inactive aconitase
    • Emptage, M. H., Dreyer, J.-L., Kennedy, M. C., and Beinert, H. (1983) Optical and EPR characterization of different species of active and inactive aconitase J. Biol. Chem. 258, 11106-11111
    • (1983) J. Biol. Chem. , vol.258 , pp. 11106-11111
    • Emptage, M.H.1    Dreyer, J.-L.2    Kennedy, M.C.3    Beinert, H.4
  • 9
    • 0000989147 scopus 로고    scopus 로고
    • Aconitase as Iron-Sulfur Protein, Enzyme, and Iron-Regulatory Protein
    • Beinert, H., Kennedy, M. C., and Stout, C. D. (1996) Aconitase as Iron-Sulfur Protein, Enzyme, and Iron-Regulatory Protein Chem. Rev. 96, 2335-2373 10.1021/cr950040z
    • (1996) Chem. Rev. , vol.96 , pp. 2335-2373
    • Beinert, H.1    Kennedy, M.C.2    Stout, C.D.3
  • 10
    • 0020807941 scopus 로고
    • Mössbauer and EPR studies of activated aconitase: Development of a localized valence state at a subsite of the [4Fe-4S] cluster on binding of citrate
    • Emptage, M. H., Kent, T. A., Kennedy, M. C., Beinert, H., and Munck, E. (1983) Mössbauer and EPR studies of activated aconitase: development of a localized valence state at a subsite of the [4Fe-4S] cluster on binding of citrate Proc. Natl. Acad. Sci. U. S. A. 80, 4674-4678 10.1073/pnas.80.15.4674
    • (1983) Proc. Natl. Acad. Sci. U. S. A. , vol.80 , pp. 4674-4678
    • Emptage, M.H.1    Kent, T.A.2    Kennedy, M.C.3    Beinert, H.4    Munck, E.5
  • 11
    • 0026587755 scopus 로고
    • Crystal structures of aconitase with isocitrate and nitroisocitrate bound
    • Lauble, H., Kennedy, M. C., Beinert, H., and Stout, C. D. (1992) Crystal structures of aconitase with isocitrate and nitroisocitrate bound Biochemistry 31, 2735-2748 10.1021/bi00125a014
    • (1992) Biochemistry , vol.31 , pp. 2735-2748
    • Lauble, H.1    Kennedy, M.C.2    Beinert, H.3    Stout, C.D.4
  • 12
    • 0033436322 scopus 로고    scopus 로고
    • The Mechanism of Aconitase: 1.8 a Resolution Crystal Structure of the S642A:Citrate Complex
    • Lloyd, S. J., Lauble, L., Prasad, G. S., and Stout, C. D. (1999) The Mechanism of Aconitase: 1.8 A Resolution Crystal Structure of the S642A:Citrate Complex Protein Sci. 8, 2655-2662 10.1110/ps.8.12.2655
    • (1999) Protein Sci. , vol.8 , pp. 2655-2662
    • Lloyd, S.J.1    Lauble, L.2    Prasad, G.S.3    Stout, C.D.4
  • 13
    • 0027375778 scopus 로고
    • The inactivation of dihydroxy-acid dehydratase in Escherichia coli treated with hyperbaric oxygen occurs because of the destruction of its Fe-S cluster, but the enzyme remains in the cell in a form that can be reactivated
    • Flint, D. H., Smyk-Randall, E., Tuminello, J. F., Draczynska-Lusiak, B., and Brown, O. R. (1993) The inactivation of dihydroxy-acid dehydratase in Escherichia coli treated with hyperbaric oxygen occurs because of the destruction of its Fe-S cluster, but the enzyme remains in the cell in a form that can be reactivated J. Biol. Chem. 268, 25547-25552
    • (1993) J. Biol. Chem. , vol.268 , pp. 25547-25552
    • Flint, D.H.1    Smyk-Randall, E.2    Tuminello, J.F.3    Draczynska-Lusiak, B.4    Brown, O.R.5
  • 14
    • 0037214441 scopus 로고    scopus 로고
    • Contrasting sensitivities of Escherichia coli aconitases a and B to oxidation and iron depletion
    • Varghese, S., Tang, Y., and Imlay, J. A. (2003) Contrasting sensitivities of Escherichia coli aconitases A and B to oxidation and iron depletion J. Bacteriol. 185, 221-230 10.1128/JB.185.1.221-230.2003
    • (2003) J. Bacteriol. , vol.185 , pp. 221-230
    • Varghese, S.1    Tang, Y.2    Imlay, J.A.3
  • 15
    • 0027491617 scopus 로고
    • The inactivation of Fe-S cluster containing hydro-lyases by superoxide
    • Flint, D. H., Tuminello, J. F., and Emptage, M. H. (1993) The inactivation of Fe-S cluster containing hydro-lyases by superoxide J. Biol. Chem. 268, 22369-22376
    • (1993) J. Biol. Chem. , vol.268 , pp. 22369-22376
    • Flint, D.H.1    Tuminello, J.F.2    Emptage, M.H.3
  • 16
    • 84915750182 scopus 로고    scopus 로고
    • Structure of L-serine dehydratase from Legionella pneumophila: Novel use of the C-terminal cysteine as an intrinsic competitive inhibitor
    • Thoden, J. B., Holden, H. M., and Grant, G. A. (2014) Structure of L-serine dehydratase from Legionella pneumophila: Novel use of the C-terminal cysteine as an intrinsic competitive inhibitor Biochemistry 53, 7615-7624 10.1021/bi501253w
    • (2014) Biochemistry , vol.53 , pp. 7615-7624
    • Thoden, J.B.1    Holden, H.M.2    Grant, G.A.3
  • 17
    • 84863531194 scopus 로고    scopus 로고
    • Allosteric activation and contrasting properties of L-serine dehydratase types 1 and 2
    • Chen, S., Xu, X. L., and Grant, G. A. (2012) Allosteric activation and contrasting properties of L-serine dehydratase types 1 and 2 Biochemistry 51, 5320-5328 10.1021/bi300523p
    • (2012) Biochemistry , vol.51 , pp. 5320-5328
    • Chen, S.1    Xu, X.L.2    Grant, G.A.3
  • 18
    • 84887097031 scopus 로고    scopus 로고
    • Identification and characterization of two new types of bacterial l-serine dehydratases and assessment of the function of the ACT domain
    • Xu, X. L. and Grant, G. A. (2013) Identification and characterization of two new types of bacterial l-serine dehydratases and assessment of the function of the ACT domain Arch. Biochem. Biophys. 540, 62-69 10.1016/j.abb.2013.10.009
    • (2013) Arch. Biochem. Biophys. , vol.540 , pp. 62-69
    • Xu, X.L.1    Grant, G.A.2
  • 19
    • 84865795514 scopus 로고    scopus 로고
    • Kinetic evidence of a noncatalytic substrate binding site that regulates activity in Legionella pneumophila L-serine dehydratase
    • Grant, G. A. (2012) Kinetic evidence of a noncatalytic substrate binding site that regulates activity in Legionella pneumophila L-serine dehydratase Biochemistry 51, 6961-6967 10.1021/bi3008774
    • (2012) Biochemistry , vol.51 , pp. 6961-6967
    • Grant, G.A.1
  • 20
    • 84926221482 scopus 로고    scopus 로고
    • Interplay between oxygen and Fe-S cluster biogenesis: Insights from the SUF pathway
    • Boyd, E. S., Thomas, K. M., Dai, Y., Boyd, J. M., and Outten, F. W. (2014) Interplay between oxygen and Fe-S cluster biogenesis: Insights from the SUF pathway Biochemistry 53, 5834-5847 10.1021/bi500488r
    • (2014) Biochemistry , vol.53 , pp. 5834-5847
    • Boyd, E.S.1    Thomas, K.M.2    Dai, Y.3    Boyd, J.M.4    Outten, F.W.5
  • 23
    • 84925285506 scopus 로고    scopus 로고
    • Mammalian iron-sulfur proteins: Novel insights into biogenesis and function
    • Rouault, T. A. (2014) Mammalian iron-sulfur proteins: Novel insights into biogenesis and function Nat. Rev. Mol. Cell Biol. 16, 45-55 10.1038/nrm3909
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.16 , pp. 45-55
    • Rouault, T.A.1
  • 24
    • 84930051032 scopus 로고    scopus 로고
    • Iron-sulfur cluster biogenesis in mammalian cells: New insights into the molecular mechanisms of cluster delivery
    • Maio, N. and Rouault, T. A. (2015) Iron-sulfur cluster biogenesis in mammalian cells: New insights into the molecular mechanisms of cluster delivery Biochim. Biophys. Acta, Mol. Cell Res. 1853, 1493-1512 10.1016/j.bbamcr.2014.09.009
    • (2015) Biochim. Biophys. Acta, Mol. Cell Res. , vol.1853 , pp. 1493-1512
    • Maio, N.1    Rouault, T.A.2
  • 25
    • 84897000909 scopus 로고    scopus 로고
    • Mitochondrial iron-sulfur protein biogenesis and human disease
    • Stehling, O., Wilbrecht, C., and Lill, R. (2014) Mitochondrial iron-sulfur protein biogenesis and human disease Biochimie 100, 61-77 10.1016/j.biochi.2014.01.010
    • (2014) Biochimie , vol.100 , pp. 61-77
    • Stehling, O.1    Wilbrecht, C.2    Lill, R.3
  • 26
    • 63049105321 scopus 로고    scopus 로고
    • MassMatrix: A database search program for rapid characterization of proteins and peptides from tandem mass spectrometry data
    • Xu, H. and Freitas, M. A. (2009) MassMatrix: a database search program for rapid characterization of proteins and peptides from tandem mass spectrometry data Proteomics 9, 1548-1555 10.1002/pmic.200700322
    • (2009) Proteomics , vol.9 , pp. 1548-1555
    • Xu, H.1    Freitas, M.A.2
  • 28
    • 0027529263 scopus 로고
    • Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation
    • Zhang, Z. and Smith, D. L. (1993) Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation Protein Sci. 2, 522-53 10.1002/pro.5560020404
    • (1993) Protein Sci. , vol.2 , pp. 522-553
    • Zhang, Z.1    Smith, D.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.