메뉴 건너뛰기




Volumn 193, Issue 4, 2011, Pages 887-895

FAD binding by ApbE protein from Salmonella enterica: A new class of FAD-binding proteins

Author keywords

[No Author keywords available]

Indexed keywords

NITROGEN; NITROUS OXIDE; PERIPLASMIC BINDING PROTEIN; PROTEIN APBE; UNCLASSIFIED DRUG;

EID: 79551479297     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00730-10     Document Type: Article
Times cited : (27)

References (40)
  • 1
    • 0034636795 scopus 로고    scopus 로고
    • IscU as a scaffold for iron-sulfur cluster biosynthesis: Sequential assembly of [2Fe-2S] and [4Fe-4S] clusters in IscU
    • Agar, J. N., et al. 2000. IscU as a scaffold for iron-sulfur cluster biosynthesis: sequential assembly of [2Fe-2S] and [4Fe-4S] clusters in IscU. Biochemistry 39:7856-7862.
    • (2000) Biochemistry , vol.39 , pp. 7856-7862
    • Agar, J.N.1
  • 2
    • 54849405513 scopus 로고    scopus 로고
    • Covalent binding of flavins to RnfG and RnfD in the Rnf complex from Vibrio cholerae
    • Backiel, J., et al. 2008. Covalent binding of flavins to RnfG and RnfD in the Rnf complex from Vibrio cholerae. Biochemistry 47:11273-11284.
    • (2008) Biochemistry , vol.47 , pp. 11273-11284
    • Backiel, J.1
  • 3
    • 0017030513 scopus 로고
    • New approach to the cultivation of methanogenic bacteria: 2-mercaptoethanesulfonic acid-dependent growth of Methanobacterium ruminantium in a pressurized atmosphere
    • Balch, W. E., and R. S. Wolfe. 1976. New approach to the cultivation of methanogenic bacteria: 2-mercaptoethanesulfonic acid-dependent growth of Methanobacterium ruminantium in a pressurized atmosphere. Appl. Environ. Microbiol. 32:781-791.
    • (1976) Appl. Environ. Microbiol. , vol.32 , pp. 781-791
    • Balch, W.E.1    Wolfe, R.S.2
  • 4
    • 0025778670 scopus 로고
    • Construction and properties of a family of pACYC184-derived cloning vectors compatible with pBR322 and its derivatives
    • Bartolomé, B., Y. Jubete, E. Martinez, and F. de la Cruz. 1991. Construction and properties of a family of pACYC184-derived cloning vectors compatible with pBR322 and its derivatives. Gene 102:75-78.
    • (1991) Gene , vol.102 , pp. 75-78
    • Bartolomé, B.1    Jubete, Y.2    Martinez, E.3    De La Cruz, F.4
  • 5
    • 0031929614 scopus 로고    scopus 로고
    • The apbE gene encodes a lipoprotein involved in thiamine synthesis in Salmonella typhimurium
    • Beck, B. J., and D. M. Downs. 1998. The apbE gene encodes a lipoprotein involved in thiamine synthesis in Salmonella typhimurium. J. Bacteriol. 180:885-891.
    • (1998) J. Bacteriol. , vol.180 , pp. 885-891
    • Beck, B.J.1    Downs, D.M.2
  • 6
    • 0032720313 scopus 로고    scopus 로고
    • A periplasmic location is essential for the role of the ApbE lipoprotein in thiamine synthesis in Salmonella typhimurium
    • Beck, B. J., and D. M. Downs. 1999. A periplasmic location is essential for the role of the ApbE lipoprotein in thiamine synthesis in Salmonella typhimurium. J. Bacteriol. 181:7285-7290.
    • (1999) J. Bacteriol. , vol.181 , pp. 7285-7290
    • Beck, B.J.1    Downs, D.M.2
  • 8
    • 0347325071 scopus 로고    scopus 로고
    • Lysogeny at mid-twentieth century: P1, P2, and other experimental systems
    • Bertani, G. 2004. Lysogeny at mid-twentieth century: P1, P2, and other experimental systems. J. Bacteriol. 186:595-600.
    • (2004) J. Bacteriol. , vol.186 , pp. 595-600
    • Bertani, G.1
  • 9
    • 84873799110 scopus 로고
    • Studies on lysogenesis. I. The mode of phage liberation by lysogenic Escherichia coli
    • Bertani, G. 1951. Studies on lysogenesis. I. The mode of phage liberation by lysogenic Escherichia coli. J. Bacteriol. 62:293-300.
    • (1951) J. Bacteriol. , vol.62 , pp. 293-300
    • Bertani, G.1
  • 10
    • 58649101413 scopus 로고    scopus 로고
    • Bacterial ApbC protein has two biochemical activities that are required for in vivo function
    • Boyd, J. M., J. L. Sondelski, and D. M. Downs. 2009. Bacterial ApbC protein has two biochemical activities that are required for in vivo function. J. Biol. Chem. 284:110-118.
    • (2009) J. Biol. Chem. , vol.284 , pp. 110-118
    • Boyd, J.M.1    Sondelski, J.L.2    Downs, D.M.3
  • 11
    • 0030846054 scopus 로고    scopus 로고
    • A new nos gene downstream from nosDFY is essential for dissimilatory reduction of nitrous oxide by Rhizobium (Sinorhizobium) meloti
    • Chan, Y. K., W. A. McCormick, and R. J. Watson. 1997. A new nos gene downstream from nosDFY is essential for dissimilatory reduction of nitrous oxide by Rhizobium (Sinorhizobium) meloti. Microbiology 143:2817-2824.
    • (1997) Microbiology , vol.143 , pp. 2817-2824
    • Chan, Y.K.1    McCormick, W.A.2    Watson, R.J.3
  • 12
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, N
    • Collaborative Computational Project, N. 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50:760-763.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 13
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: All-atom contacts and structure validation for proteins and nucleic acids
    • Davis, I. W., et al. 2007. MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res. 35:W375-W383.
    • (2007) Nucleic Acids Res. , vol.35
    • Davis, I.W.1
  • 14
    • 0003455675 scopus 로고
    • and Cold Spring Harbor Laboratory Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • Davis, R. W., D. Botstein, J. R. Roth, and Cold Spring Harbor Laboratory. 1980. Advanced bacterial genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
    • (1980) Advanced Bacterial Genetics
    • Davis, R.W.1    Botstein, D.2    Roth, J.R.3
  • 16
    • 0034854206 scopus 로고    scopus 로고
    • Sequence-structure analysis of FAD-containing proteins
    • Dym, O., and D. Eisenberg. 2001. Sequence-structure analysis of FAD-containing proteins. Protein Sci. 10:1712-1728.
    • (2001) Protein Sci. , vol.10 , pp. 1712-1728
    • Dym, O.1    Eisenberg, D.2
  • 19
    • 0038419597 scopus 로고    scopus 로고
    • The YggX protein of Salmonella enterica is involved in Fe(II) trafficking and minimizes the DNA damage caused by hydroxyl radicals: Residue CYS-7 is essential for YggX function
    • Gralnick, J. A., and D. M. Downs. 2003. The YggX protein of Salmonella enterica is involved in Fe(II) trafficking and minimizes the DNA damage caused by hydroxyl radicals: residue CYS-7 is essential for YggX function. J. Biol. Chem. 278:20708-20715.
    • (2003) J. Biol. Chem. , vol.278 , pp. 20708-20715
    • Gralnick, J.A.1    Downs, D.M.2
  • 20
    • 0036142325 scopus 로고    scopus 로고
    • A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p
    • Gross, E., C. Sevier, A. Vala, C. Kaiser, and D. Fass. 2002. A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p. Nat. Struct. Biol. 9:61-67.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 61-67
    • Gross, E.1    Sevier, C.2    Vala, A.3    Kaiser, C.4    Fass, D.5
  • 21
    • 33748443040 scopus 로고    scopus 로고
    • Crystal structure of the ApbE protein (TM1553) from Thermotoga maritima at 1.58 Å resolution
    • Han, G. W., et al. 2006. Crystal structure of the ApbE protein (TM1553) from Thermotoga maritima at 1.58 Å resolution. Proteins 64:1083-1090.
    • (2006) Proteins , vol.64 , pp. 1083-1090
    • Han, G.W.1
  • 22
    • 0242267926 scopus 로고    scopus 로고
    • Deflavination and reconstitution of flavoproteins
    • Hefti, M. H., J. Vervoort, and W. J. van Berkel. 2003. Deflavination and reconstitution of flavoproteins. Eur. J. Biochem. 270:4227-4242.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 4227-4242
    • Hefti, M.H.1    Vervoort, J.2    Van Berkel, W.J.3
  • 23
    • 0029918694 scopus 로고    scopus 로고
    • The FSSP database: Fold classification based on structure-structure alignment of proteins
    • Holm, L., and C. Sander. 1996. The FSSP database: fold classification based on structure-structure alignment of proteins. Nucleic Acids Res. 24:206-209.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 206-209
    • Holm, L.1    Sander, C.2
  • 24
    • 0015187451 scopus 로고
    • Localized mutagenesis of any specific small region of the bacterial chromosome
    • Hong, J. S., and B. N. Ames. 1971. Localized mutagenesis of any specific small region of the bacterial chromosome. Proc. Natl. Acad. Sci. U. S. A. 68:3158-3162.
    • (1971) Proc. Natl. Acad. Sci. U. S. A. , vol.68 , pp. 3158-3162
    • Hong, J.S.1    Ames, B.N.2
  • 25
    • 60649087951 scopus 로고    scopus 로고
    • Production, characterization and determination of the real catalytic properties of the putative succinate dehydrogenase from Wolinella succinogenes
    • Juhnke, H. D., H. Hiltscher, H. R. Nasiri, H. Schwalbe, and C. R. Lancaster. 2009. Production, characterization and determination of the real catalytic properties of the putative 'succinate dehydrogenase' from Wolinella succinogenes. Mol. Microbiol. 71:1088-1101.
    • (2009) Mol. Microbiol. , vol.71 , pp. 1088-1101
    • Juhnke, H.D.1    Hiltscher, H.2    Nasiri, H.R.3    Schwalbe, H.4    Lancaster, C.R.5
  • 26
    • 0026023225 scopus 로고
    • + reductase: Prototype for a structurally novel flavoenzyme family
    • + reductase: prototype for a structurally novel flavoenzyme family. Science 251:60-66.
    • (1991) Science , vol.251 , pp. 60-66
    • Karplus, P.A.1    Daniels, M.J.2    Herriott, J.R.3
  • 27
    • 0038540118 scopus 로고    scopus 로고
    • A reducing system of the superoxide sensor SoxR in Escherichia coli
    • Koo, M. S., et al. 2003. A reducing system of the superoxide sensor SoxR in Escherichia coli. EMBO J. 22:2614-2622.
    • (2003) EMBO J. , vol.22 , pp. 2614-2622
    • Koo, M.S.1
  • 29
    • 34547787056 scopus 로고    scopus 로고
    • Tricarballylate catabolism in Salmonella enterica. The TcuB protein uses 4Fe-4S clusters and heme to transfer electrons from FADH2 in the tricarballylate dehydrogenase (TcuA) enzyme to electron acceptors in the cell membrane
    • Lewis, J. A., and J. C. Escalante-Semerena. 2007. Tricarballylate catabolism in Salmonella enterica. The TcuB protein uses 4Fe-4S clusters and heme to transfer electrons from FADH2 in the tricarballylate dehydrogenase (TcuA) enzyme to electron acceptors in the cell membrane. Biochemistry 46:9107-9115.
    • (2007) Biochemistry , vol.46 , pp. 9107-9115
    • Lewis, J.A.1    Escalante-Semerena, J.C.2
  • 30
    • 10044259795 scopus 로고    scopus 로고
    • Role of a nosX homolog in Streptococcus gordonii in aerobic growth and biofilm formation
    • Loo, C. Y., et al. 2004. Role of a nosX homolog in Streptococcus gordonii in aerobic growth and biofilm formation. J. Bacteriol. 186:8193-8206.
    • (2004) J. Bacteriol. , vol.186 , pp. 8193-8206
    • Loo, C.Y.1
  • 31
    • 0032619605 scopus 로고    scopus 로고
    • UV-visible spectroscopy as a tool to study flavoproteins
    • Macheroux, P. 1999. UV-visible spectroscopy as a tool to study flavoproteins. Methods Mol. Biol. 131:1-7.
    • (1999) Methods Mol. Biol. , vol.131 , pp. 1-7
    • Macheroux, P.1
  • 32
    • 0033851115 scopus 로고    scopus 로고
    • The chemical and biological versatility of riboflavin
    • Massey, V. 2000. The chemical and biological versatility of riboflavin. Biochem. Soc. Trans. 28:283-296.
    • (2000) Biochem. Soc. Trans. , vol.28 , pp. 283-296
    • Massey, V.1
  • 35
    • 65349091597 scopus 로고    scopus 로고
    • A periplasmic aldehyde oxidoreductase represents the first molybdopterin cytosine dinucleotide cofactor containing molybdo- Flavoenzyme from Escherichia coli
    • Neumann, M., et al. 2009. A periplasmic aldehyde oxidoreductase represents the first molybdopterin cytosine dinucleotide cofactor containing molybdo- flavoenzyme from Escherichia coli. FEBS J. 276:2762-2774.
    • (2009) FEBS J. , vol.276 , pp. 2762-2774
    • Neumann, M.1
  • 36
    • 0027131592 scopus 로고
    • Identification of a new class of nitrogen fixation genes in Rhodobacter capsulatus: A putative membrane complex involved in electron transport to nitrogenase
    • Schmehl, M., et al. 1993. Identification of a new class of nitrogen fixation genes in Rhodobacter capsulatus: a putative membrane complex involved in electron transport to nitrogenase. Mol. Gen. Genet. 241:602-615.
    • (1993) Mol. Gen. Genet. , vol.241 , pp. 602-615
    • Schmehl, M.1
  • 37
    • 0020414542 scopus 로고
    • FAD-binding site of glutathione reductase
    • Schulz, G. E., R. H. Schirmer, and E. F. Pai. 1982. FAD-binding site of glutathione reductase. J. Mol. Biol. 160:287-308.
    • (1982) J. Mol. Biol. , vol.160 , pp. 287-308
    • Schulz, G.E.1    Schirmer, R.H.2    Pai, E.F.3
  • 38
    • 0037216551 scopus 로고    scopus 로고
    • Lack of the ApbC or ApbE protein results in a defect in Fe-S cluster metabolism in Salmonella enterica serovar Typhimurium
    • Skovran, E., and D. M. Downs. 2003. Lack of the ApbC or ApbE protein results in a defect in Fe-S cluster metabolism in Salmonella enterica serovar Typhimurium. J. Bacteriol. 185:98-106.
    • (2003) J. Bacteriol. , vol.185 , pp. 98-106
    • Skovran, E.1    Downs, D.M.2
  • 39
    • 77049313195 scopus 로고
    • Acetylornithase of Escherichia coli: Partial purification and some properties
    • Vogel, H. J., and D. M. Bonner. 1956. Acetylornithase of Escherichia coli: partial purification and some properties. J. Biol. Chem. 218:97-106.
    • (1956) J. Biol. Chem. , vol.218 , pp. 97-106
    • Vogel, H.J.1    Bonner, D.M.2
  • 40
    • 14644397891 scopus 로고    scopus 로고
    • Functional domains of NosR, a novel transmembrane iron-sulfur flavoprotein necessary for nitrous oxide respiration
    • Wunsch, P., and W. G. Zumft. 2005. Functional domains of NosR, a novel transmembrane iron-sulfur flavoprotein necessary for nitrous oxide respiration. J. Bacteriol. 187:1992-2001.
    • (2005) J. Bacteriol. , vol.187 , pp. 1992-2001
    • Wunsch, P.1    Zumft, W.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.