메뉴 건너뛰기




Volumn 262, Issue 2, 1999, Pages 396-405

Phospholipid bound to the flavohemoprotein from Alcaligenes eutrophus

Author keywords

Crystal structure; Flavohemoprotein; Globin; Phospholipid; Protein engineering

Indexed keywords

ETHANOLAMINE DERIVATIVE; FLAVOPROTEIN; GLYCEROL DERIVATIVE; GLYCEROPHOSPHATE; HEMOPROTEIN; OXIDOREDUCTASE; PHOSPHOLIPID; PHOSPHOLIPID BINDING PROTEIN;

EID: 0033152098     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00381.x     Document Type: Article
Times cited : (44)

References (49)
  • 1
    • 0028242684 scopus 로고
    • Primary sequence and evidence for a physiological function of the flavohemoprotein of Alcaligenes eutrophus
    • 1. Cramm, R., Siddiqui, R.A. & Friedrich, B. (1994) Primary sequence and evidence for a physiological function of the flavohemoprotein of Alcaligenes eutrophus. J. Biol. Chem. 269, 7349-7354.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7349-7354
    • Cramm, R.1    Siddiqui, R.A.2    Friedrich, B.3
  • 2
    • 0025764867 scopus 로고
    • Isolation and nucleotide sequence of the hmp gene that encodes a haemoglobin-like protein in Escherichia coli K-12
    • 2. Vasudevan, S.G., Armarego, W.L.F., Shaw, D.C.P., Lilley, E., Dixon, N.E. & Poole, R.K. (1991) Isolation and nucleotide sequence of the hmp gene that encodes a haemoglobin-like protein in Escherichia coli K-12. Mol. Gen. Genet. 226, 49-58.
    • (1991) Mol. Gen. Genet. , vol.226 , pp. 49-58
    • Vasudevan, S.G.1    Armarego, W.L.F.2    Shaw, D.C.P.3    Lilley, E.4    Dixon, N.E.5    Poole, R.K.6
  • 3
    • 0032524650 scopus 로고    scopus 로고
    • Role for the Salmonella flavohemoglobin in protection from nitric oxide
    • 3. Crawford, M.J. & Goldberg, D.E. (1998) Role for the Salmonella flavohemoglobin in protection from nitric oxide. J. Biol. Chem. 273, 12543-12547.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12543-12547
    • Crawford, M.J.1    Goldberg, D.E.2
  • 4
    • 0029002203 scopus 로고
    • Flavohaemoglobin HmpX: A new pathogenicity determinant in Erwinia chrysanthemi strain 3937
    • 4. Favey, S., Labesse, G., Vouille, V. & Boccara, M. (1995) Flavohaemoglobin HmpX: a new pathogenicity determinant in Erwinia chrysanthemi strain 3937. Microbiology 141, 863-871.
    • (1995) Microbiology , vol.141 , pp. 863-871
    • Favey, S.1    Labesse, G.2    Vouille, V.3    Boccara, M.4
  • 5
    • 0029967350 scopus 로고    scopus 로고
    • Oxygen-controlled regulation of the flavohemoglobin gene in Bacillus subtilis
    • 5. Lacelle, M., Kumano, M., Kurita, K., Yamane, K., Zuber, P. & Nakano, M.M. (1996) Oxygen-controlled regulation of the flavohemoglobin gene in Bacillus subtilis. J. Bacteriol. 178, 3803-3808.
    • (1996) J. Bacteriol. , vol.178 , pp. 3803-3808
    • Lacelle, M.1    Kumano, M.2    Kurita, K.3    Yamane, K.4    Zuber, P.5    Nakano, M.M.6
  • 6
    • 0028018360 scopus 로고
    • MotX, the channel component of the sodium type flagellar motor
    • 6. McCarter, L.M. (1994) MotX, the channel component of the sodium type flagellar motor. J. Bacteriol. 176, 5988-5998.
    • (1994) J. Bacteriol. , vol.176 , pp. 5988-5998
    • McCarter, L.M.1
  • 7
    • 0026651286 scopus 로고
    • Yeast flavohemoglobin is an ancient protein related to globins and a reductase family
    • 7. Zhu, H. & Riggs, A.F. (1992) Yeast flavohemoglobin is an ancient protein related to globins and a reductase family. Proc. Natl Acad. Sci. USA 89, 5015-5019.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 5015-5019
    • Zhu, H.1    Riggs, A.F.2
  • 8
    • 0026802281 scopus 로고
    • Amino acid sequence of yeast hemoglobin
    • 8. Iwaasa, H., Tagaki, T. & Shikama, K. (1992) Amino acid sequence of yeast hemoglobin. J. Mol. Biol. 227, 948-954.
    • (1992) J. Mol. Biol. , vol.227 , pp. 948-954
    • Iwaasa, H.1    Tagaki, T.2    Shikama, K.3
  • 9
    • 0030799397 scopus 로고    scopus 로고
    • Purification and characterization of a flavohemoglobin from the denitrifying fungus Fusarium oxysporum
    • 9. Takaya, N., Suwaki, S., Matsuo, M. & Hirofumi, S. (1997) Purification and characterization of a flavohemoglobin from the denitrifying fungus Fusarium oxysporum. FEBS 414, 545-548.
    • (1997) FEBS , vol.414 , pp. 545-548
    • Takaya, N.1    Suwaki, S.2    Matsuo, M.3    Hirofumi, S.4
  • 11
    • 0017068536 scopus 로고
    • Respiratory components and oxidase activities in Alcaligenes eutrophus
    • 11. Probst, I. & Schlegel, H.G. (1976) Respiratory components and oxidase activities in Alcaligenes eutrophus. Biochim. Biophys. Acta 440, 412-428.
    • (1976) Biochim. Biophys. Acta , vol.440 , pp. 412-428
    • Probst, I.1    Schlegel, H.G.2
  • 12
    • 0018801772 scopus 로고
    • An oxygen-binding flavohemoprotein from Alcaligenes eutrophus
    • 12. Probst, I., Wolf, G. & Schlegel, H.G. (1979) An oxygen-binding flavohemoprotein from Alcaligenes eutrophus. Biochim. Biophys. Acta 576, 471-478.
    • (1979) Biochim. Biophys. Acta , vol.576 , pp. 471-478
    • Probst, I.1    Wolf, G.2    Schlegel, H.G.3
  • 13
    • 0029610660 scopus 로고
    • Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 Å resolution
    • 13. Ermler, U., Siddiqui, R.A., Gramm, R. & Friedrich, B. (1995) Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 Å resolution. EMBO J. 24, 6067-6077.
    • (1995) EMBO J. , vol.24 , pp. 6067-6077
    • Ermler, U.1    Siddiqui, R.A.2    Gramm, R.3    Friedrich, B.4
  • 14
  • 15
    • 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
  • 23
    • 0028483212 scopus 로고
    • Structure of a human Clara cell phospholipid-binding protein-ligand complex at 1.9 Å resolution
    • 23. Umland, T.C., Swaminathan, S., Singh, G., Warty, V., Furey, W., Pletcher, J. & Sax, M. (1994) Structure of a human Clara cell phospholipid-binding protein-ligand complex at 1.9 Å resolution. Nat. Struct. Biol. 1, 538-545.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 538-545
    • Umland, T.C.1    Swaminathan, S.2    Singh, G.3    Warty, V.4    Furey, W.5    Pletcher, J.6    Sax, M.7
  • 24
    • 0032576758 scopus 로고    scopus 로고
    • Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol-transfer protein
    • 24. Sha, B., Philips, S.E., Bankaitis, V.A. & Ming, L. (1998) Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol-transfer protein. Nature 391, 506-510.
    • (1998) Nature , vol.391 , pp. 506-510
    • Sha, B.1    Philips, S.E.2    Bankaitis, V.A.3    Ming, L.4
  • 25
    • 0030760314 scopus 로고    scopus 로고
    • Crystal structure of human BPI and two bound phospholipids at 2.4 Å resolution
    • 25. Beamer, L., Carroll, S.F. & Eisenberg, D. (1997) Crystal structure of human BPI and two bound phospholipids at 2.4 Å resolution. Science 276, 1861-1864.
    • (1997) Science , vol.276 , pp. 1861-1864
    • Beamer, L.1    Carroll, S.F.2    Eisenberg, D.3
  • 26
    • 0032527992 scopus 로고    scopus 로고
    • The structural basis of lipid interactions in lipovitellin, a soluble lipoprotein
    • 26. Anderson, T.A., Levitt, D.G. & Banaszak, L.J. (1998) The structural basis of lipid interactions in lipovitellin, a soluble lipoprotein. Structure 6, 895-909.
    • (1998) Structure , vol.6 , pp. 895-909
    • Anderson, T.A.1    Levitt, D.G.2    Banaszak, L.J.3
  • 28
    • 0027410046 scopus 로고
    • The pRSET family of T7 promoter expression vectors for Escherichia coli
    • 28. Schoepfer, R. (1993) The pRSET family of T7 promoter expression vectors for Escherichia coli. Gene 124, 83-85.
    • (1993) Gene , vol.124 , pp. 83-85
    • Schoepfer, R.1
  • 30
    • 0026573580 scopus 로고
    • A general and fast method to generate multiple site-directed mutations
    • 30. Mikaelian, I. & Sergant, A. (1992) A general and fast method to generate multiple site-directed mutations. Nucleic Acids Res. 20, 376-376.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 376-376
    • Mikaelian, I.1    Sergant, A.2
  • 31
    • 0025026382 scopus 로고
    • Hemoglobins of the Lucina pectinata/bacteria symbiosis. I. Molecular properties, kinetics and equilibria of reactions with ligands
    • 31. Kraus, D.W. & Wittenberg, J.B. (1990) Hemoglobins of the Lucina pectinata/bacteria symbiosis. I. Molecular properties, kinetics and equilibria of reactions with ligands. J. Biol. Chem. 265, 16043-16053.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16043-16053
    • Kraus, D.W.1    Wittenberg, J.B.2
  • 32
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • 32. Bligh, E.G. & Dyer, W.J. (1959) A rapid method of total lipid extraction and purification. Can. J. Biochem. Phys. 37, 911-915.
    • (1959) Can. J. Biochem. Phys. , vol.37 , pp. 911-915
    • Bligh, E.G.1    Dyer, W.J.2
  • 33
    • 0025687382 scopus 로고
    • A new and rapid method for the assay of bacterial fatty acids using high resolution capillary gas chromatography and trimethylsulfonium hydroxide
    • 33. Müller, K.-D., Husmann, H. & Nalik, H.P. (1990) A new and rapid method for the assay of bacterial fatty acids using high resolution capillary gas chromatography and trimethylsulfonium hydroxide. Zbl. Bakt. 274, 174-182.
    • (1990) Zbl. Bakt. , vol.274 , pp. 174-182
    • Müller, K.-D.1    Husmann, H.2    Nalik, H.P.3
  • 34
    • 0343879238 scopus 로고
    • Assay of inorganic phosphate, total phosphate and phosphatases
    • 34. Ames, B.N. (1966) Assay of inorganic phosphate, total phosphate and phosphatases. Methods Enzymol. 8, 115-118.
    • (1966) Methods Enzymol. , vol.8 , pp. 115-118
    • Ames, B.N.1
  • 35
    • 0029057180 scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of a bacterial flavohemoglobin from Alcaligenes eutrophus
    • 35. Ermler, U., Siddiqui, R.A., Cramm, R., Schröder, D. & Friedrich, B. (1995) Crystallization and preliminary X-ray diffraction studies of a bacterial flavohemoglobin from Alcaligenes eutrophus. Proteins 21, 351-353.
    • (1995) Proteins , vol.21 , pp. 351-353
    • Ermler, U.1    Siddiqui, R.A.2    Cramm, R.3    Schröder, D.4    Friedrich, B.5
  • 36
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • 36. Jones, T.A., Zou, J.-Y., Cowan, S. & Kieldgaard, M. (1991) Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47, 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.3    Kieldgaard, M.4
  • 37
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • 37. Brünger, A.T., Kuriyan, J. & Karplus, M. (1987) Crystallographic R factor refinement by molecular dynamics. Science 235, 458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 38
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • 38. Otwinowski, Z. & Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 39
    • 0026470012 scopus 로고
    • Spectroscopic studies on an oxygen-binding haemoglobin-like flavohaemoprotein from Escherichia coli
    • 39. Ioannidis, N., Cooper, C.E. & Poole, R.K. (1992) Spectroscopic studies on an oxygen-binding haemoglobin-like flavohaemoprotein from Escherichia coli. Biochem. J. 288, 649-655.
    • (1992) Biochem. J. , vol.288 , pp. 649-655
    • Ioannidis, N.1    Cooper, C.E.2    Poole, R.K.3
  • 40
  • 41
    • 0016236836 scopus 로고
    • Spectral characteristics and interconversions of the reduced, oxidized, and oxygenated forms of purified cytochrome o
    • 41. Liu, C.Y. & Webster, D.A. (1973) Spectral characteristics and interconversions of the reduced, oxidized, and oxygenated forms of purified cytochrome o. J. Biol. Chem. 249, 4261-4266.
    • (1973) J. Biol. Chem. , vol.249 , pp. 4261-4266
    • Liu, C.Y.1    Webster, D.A.2
  • 42
    • 0030221278 scopus 로고    scopus 로고
    • The different conformations of the glycerol region of crystalline acylglycerols
    • 42. Pascher, I. (1996) The different conformations of the glycerol region of crystalline acylglycerols. Curr. Opin. Struct. Biol. 6, 439-448.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 439-448
    • Pascher, I.1
  • 43
    • 0023648635 scopus 로고
    • Conformation and packing properties of membrane lipids: The crystal structure of sodium dimyristoylphosphatidylglycerol
    • 43. Pascher, I., Sundell, S., Harlos, K. & Eibl, H. (1987) Conformation and packing properties of membrane lipids: the crystal structure of sodium dimyristoylphosphatidylglycerol. Biochim. Biophys. Acta 896, 77-88.
    • (1987) Biochim. Biophys. Acta , vol.896 , pp. 77-88
    • Pascher, I.1    Sundell, S.2    Harlos, K.3    Eibl, H.4
  • 44
    • 0030055628 scopus 로고    scopus 로고
    • Structural basis of light harvesting by carotenoids: Peridinin-chlorophyll-protein from Amphidiinium carterae
    • 44. Hofmann, E., Wrench, P.M., Sharpies, F.P., Hiller, R.G., Welte, W. & Diederichs, K. (1996) Structural basis of light harvesting by carotenoids: peridinin-chlorophyll-protein from Amphidiinium carterae. Science 272, 1788-1791.
    • (1996) Science , vol.272 , pp. 1788-1791
    • Hofmann, E.1    Wrench, P.M.2    Sharpies, F.P.3    Hiller, R.G.4    Welte, W.5    Diederichs, K.6
  • 45
    • 0032143907 scopus 로고    scopus 로고
    • The implications of the structure of the bactericidal/permeability protein on the lipid-transfer function of the cholesteryl ester transfer protein
    • 45. Brune, C., Beamer, L. & Tall, A.R. (1998) The implications of the structure of the bactericidal/permeability protein on the lipid-transfer function of the cholesteryl ester transfer protein. Curr. Opin. Struct. Biol. 8, 426-434.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 426-434
    • Brune, C.1    Beamer, L.2    Tall, A.R.3
  • 46
    • 0031569849 scopus 로고    scopus 로고
    • Unusual structure of the oxygen-binding site in the dimeric bacterial protein from Vitreoscilla sp
    • 46. Tarricone, C., Galizzi, A., Coda, A., Ascenzi, P. & Bolognesi, M. (1997) Unusual structure of the oxygen-binding site in the dimeric bacterial protein from Vitreoscilla sp. Structure 5, 497-507.
    • (1997) Structure , vol.5 , pp. 497-507
    • Tarricone, C.1    Galizzi, A.2    Coda, A.3    Ascenzi, P.4    Bolognesi, M.5
  • 47
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MOLSCRIPT that includes greatly enhanced coloring capabilities
    • 47. Esnouf, R.M. (1997) An extensively modified version of MOLSCRIPT that includes greatly enhanced coloring capabilities. J. Mol. Graphics 15, 133-138.
    • (1997) J. Mol. Graphics , vol.15 , pp. 133-138
    • Esnouf, R.M.1
  • 48
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • 48. Kraulis, P.J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 49
    • 0028057108 scopus 로고
    • Raster3D, version 2.0. A program for photorealistic molecular graphics
    • 49. Merrit, E.A. & Murphy, M.E.P. (1994) Raster3D, Version 2.0. A program for photorealistic molecular graphics. Acta Crystallogr. D50, 869-873.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 869-873
    • Merrit, E.A.1    Murphy, M.E.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.