메뉴 건너뛰기




Volumn 366, Issue 4, 2007, Pages 1332-1350

Limulus polyphemus Hemocyanin: 10 Å Cryo-EM Structure, Sequence Analysis, Molecular Modelling and Rigid-body Fitting Reveal the Interfaces Between the Eight Hexamers

Author keywords

3D reconstruction; amino acid sequence; cryo electron microscopy; hemocyanin; quaternary structure

Indexed keywords

AMINO ACID; HEMOCYANIN; HISTIDINE; PROTEIN SUBUNIT;

EID: 33846638741     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.11.075     Document Type: Article
Times cited : (44)

References (49)
  • 1
    • 0000222758 scopus 로고
    • Molecular structure of the arthropod hemocyanins
    • Markl J., and Decker H. Molecular structure of the arthropod hemocyanins. Advan. Comp. Environ. Physiol. 13 (1992) 325-376
    • (1992) Advan. Comp. Environ. Physiol. , vol.13 , pp. 325-376
    • Markl, J.1    Decker, H.2
  • 3
    • 33644927549 scopus 로고    scopus 로고
    • The hemocyanin from a living fossil, the cephalopod Nautilus pompilius: protein structure, gene organization, and evolution
    • Bergmann S., Lieb B., Ruth P., and Markl J. The hemocyanin from a living fossil, the cephalopod Nautilus pompilius: protein structure, gene organization, and evolution. J. Mol. Evol. 62 (2006) 362-374
    • (2006) J. Mol. Evol. , vol.62 , pp. 362-374
    • Bergmann, S.1    Lieb, B.2    Ruth, P.3    Markl, J.4
  • 4
    • 0024975122 scopus 로고
    • Crystal structure of hexameric hemocyanin from Panulirus interruptus refined at 3.2 Å resolution
    • Volbeda A., and Hol W.G.J. Crystal structure of hexameric hemocyanin from Panulirus interruptus refined at 3.2 Å resolution. J. Mol. Biol. 209 (1989) 249-279
    • (1989) J. Mol. Biol. , vol.209 , pp. 249-279
    • Volbeda, A.1    Hol, W.G.J.2
  • 5
    • 0027529265 scopus 로고
    • Crystal structure of deoxygenated Limulus polyphemus subunit II hemocyanin at 2.18 Å resolution: clues for a mechanism for allosteric regulation
    • Hazes B., Magnus K.A., Bonaventura C., Bonaventura J., Dauter Z., Kalk K.H., and Hol W.G. Crystal structure of deoxygenated Limulus polyphemus subunit II hemocyanin at 2.18 Å resolution: clues for a mechanism for allosteric regulation. Protein Sci. 2 (1993) 597-619
    • (1993) Protein Sci. , vol.2 , pp. 597-619
    • Hazes, B.1    Magnus, K.A.2    Bonaventura, C.3    Bonaventura, J.4    Dauter, Z.5    Kalk, K.H.6    Hol, W.G.7
  • 7
    • 0025821738 scopus 로고
    • Hexamers of subunit II from Limulus hemocyanin (a 48-mer) have the same quaternary structure as whole Panulirus hemocyanin molecules
    • Magnus K.A., Lattman E.E., Volbeda A., and Hol W.G.J. Hexamers of subunit II from Limulus hemocyanin (a 48-mer) have the same quaternary structure as whole Panulirus hemocyanin molecules. Proteins: Struct. Funct. Genet. 9 (1991) 240-247
    • (1991) Proteins: Struct. Funct. Genet. , vol.9 , pp. 240-247
    • Magnus, K.A.1    Lattman, E.E.2    Volbeda, A.3    Hol, W.G.J.4
  • 8
    • 4544340747 scopus 로고    scopus 로고
    • Functional changes in the family of type 3 copper proteins in evolution
    • Jaenicke E., and Decker H. Functional changes in the family of type 3 copper proteins in evolution. Chem. Biol. Chem. 5 (2004) 163-176
    • (2004) Chem. Biol. Chem. , vol.5 , pp. 163-176
    • Jaenicke, E.1    Decker, H.2
  • 9
    • 0035140529 scopus 로고    scopus 로고
    • Molecular evolution of the arthropod hemocyanin superfamily
    • Burmester T. Molecular evolution of the arthropod hemocyanin superfamily. Mol. Biol. Evol. 18 (2001) 184-195
    • (2001) Mol. Biol. Evol. , vol.18 , pp. 184-195
    • Burmester, T.1
  • 10
    • 0036934041 scopus 로고    scopus 로고
    • Origin and evolution of arthropod hemocyanins and related proteins
    • Burmester T. Origin and evolution of arthropod hemocyanins and related proteins. J. Comp. Physiol. B. 172 (2002) 95-117
    • (2002) J. Comp. Physiol. B. , vol.172 , pp. 95-117
    • Burmester, T.1
  • 12
    • 0027034441 scopus 로고
    • Quaternary and subunit structure of Calliphora arylphorin as deduced from electron microscopy, electrophoresis, and sequence similarities with arthropod hemocyanin
    • Markl J., Burmester T., Decker H., Savel-Niemann A., Harris J.R., Süling M., et al. Quaternary and subunit structure of Calliphora arylphorin as deduced from electron microscopy, electrophoresis, and sequence similarities with arthropod hemocyanin. J. Comp. Physiol. 162 (1992) 665-680
    • (1992) J. Comp. Physiol. , vol.162 , pp. 665-680
    • Markl, J.1    Burmester, T.2    Decker, H.3    Savel-Niemann, A.4    Harris, J.R.5    Süling, M.6
  • 13
    • 0000463939 scopus 로고
    • Hemocyanin in spiders, XI. The quaternary structure of Cupiennius hemocyanin
    • Markl J. Hemocyanin in spiders, XI. The quaternary structure of Cupiennius hemocyanin. J. Comp. Physiol. 140 (1980) 199-207
    • (1980) J. Comp. Physiol. , vol.140 , pp. 199-207
    • Markl, J.1
  • 14
    • 0002261584 scopus 로고
    • Evolution and function of structurally diverse subunits in the respiratory protein hemocyanin from arthropods
    • Markl J. Evolution and function of structurally diverse subunits in the respiratory protein hemocyanin from arthropods. Biol. Bull. (Woods Hole) 171 (1986) 90-115
    • (1986) Biol. Bull. (Woods Hole) , vol.171 , pp. 90-115
    • Markl, J.1
  • 15
    • 0025238635 scopus 로고
    • An approach to the architecture of Scutigera coleoptrata hemocyanin by electron microscopy and image processing
    • Boisset N., Taveau J.-C., and Lamy J.-N. An approach to the architecture of Scutigera coleoptrata hemocyanin by electron microscopy and image processing. Biol. Cell 68 (1990) 73-84
    • (1990) Biol. Cell , vol.68 , pp. 73-84
    • Boisset, N.1    Taveau, J.-C.2    Lamy, J.-N.3
  • 16
    • 0017400786 scopus 로고
    • Oxygen binding of Limulus polyphemus hemocyanin: allosteric modulation of chloride ions
    • Brouwer M., Bonaventura C., and Bonaventura J. Oxygen binding of Limulus polyphemus hemocyanin: allosteric modulation of chloride ions. Biochemistry 16 (1977) 3897-3902
    • (1977) Biochemistry , vol.16 , pp. 3897-3902
    • Brouwer, M.1    Bonaventura, C.2    Bonaventura, J.3
  • 18
    • 0020484054 scopus 로고
    • Comparison of 4x6-meric hemocyanins from three different arthropods using computer alignment and correspondence analysis
    • Bijlholt M.M.C., van Heel M.G., and van Bruggen E.F.J. Comparison of 4x6-meric hemocyanins from three different arthropods using computer alignment and correspondence analysis. J. Mol. Biol. 161 (1982) 139-153
    • (1982) J. Mol. Biol. , vol.161 , pp. 139-153
    • Bijlholt, M.M.C.1    van Heel, M.G.2    van Bruggen, E.F.J.3
  • 19
    • 0019615826 scopus 로고
    • Subunit composition of a high molecular weight oligomer: Limulus polyphemus hemocyanin
    • Brenowitz M., Bonaventura J., Bonaventura C., and Gianazza E. Subunit composition of a high molecular weight oligomer: Limulus polyphemus hemocyanin. Arch. Biochem. Biophys. 210 (1981) 748-761
    • (1981) Arch. Biochem. Biophys. , vol.210 , pp. 748-761
    • Brenowitz, M.1    Bonaventura, J.2    Bonaventura, C.3    Gianazza, E.4
  • 21
    • 0020775853 scopus 로고
    • Immunological correlates between multiple isolated subunits of Androctonus australis and Limulus polyphemus hemocyanin: an evolutionary approach
    • Lamy J., Compin S., and Lamy J.N. Immunological correlates between multiple isolated subunits of Androctonus australis and Limulus polyphemus hemocyanin: an evolutionary approach. Arch. Biochem. Biophys. 223 (1983) 584-603
    • (1983) Arch. Biochem. Biophys. , vol.223 , pp. 584-603
    • Lamy, J.1    Compin, S.2    Lamy, J.N.3
  • 22
    • 0021943132 scopus 로고
    • Immunological correspondence between arthropod hemocyanin subunits. II. Xiphosuran (Limulus) and spider (Eurypelma, Cupiennius) hemocyanin
    • Kempter B., Markl J., Brenowitz M., Bonaventura C., and Bonaventura J. Immunological correspondence between arthropod hemocyanin subunits. II. Xiphosuran (Limulus) and spider (Eurypelma, Cupiennius) hemocyanin. Biol. Chem. Hoppe Seyler 366 (1985) 77-86
    • (1985) Biol. Chem. Hoppe Seyler , vol.366 , pp. 77-86
    • Kempter, B.1    Markl, J.2    Brenowitz, M.3    Bonaventura, C.4    Bonaventura, J.5
  • 23
    • 0019891906 scopus 로고
    • Quaternary structure of scorpion (Androctonus australis) hemocyanin. Localization of subunits with immunological methods and electron microscopy
    • Lamy J., Bijlholt M.M.C., Sizaret P.-Y., Lamy J., and van Bruggen E.F.J. Quaternary structure of scorpion (Androctonus australis) hemocyanin. Localization of subunits with immunological methods and electron microscopy. Biochemistry 20 (1981) 1849-1856
    • (1981) Biochemistry , vol.20 , pp. 1849-1856
    • Lamy, J.1    Bijlholt, M.M.C.2    Sizaret, P.-Y.3    Lamy, J.4    van Bruggen, E.F.J.5
  • 24
    • 0019754921 scopus 로고
    • Hemocyanin in spiders, XVI. Subunit topography and a model of the quaternary structure of Eurypelma hemocyanin
    • Markl J., Kempter B., Linzen B., Bijlholt M.M.C., and van Bruggen E.F.J. Hemocyanin in spiders, XVI. Subunit topography and a model of the quaternary structure of Eurypelma hemocyanin. Biol. Chem. Hoppe-Seyler 362 (1981) 1631-1641
    • (1981) Biol. Chem. Hoppe-Seyler , vol.362 , pp. 1631-1641
    • Markl, J.1    Kempter, B.2    Linzen, B.3    Bijlholt, M.M.C.4    van Bruggen, E.F.J.5
  • 25
    • 0020197761 scopus 로고
    • A refined quaternary structure of Androctonus australis hemocyanin
    • Sizaret P.-Y., Frank J., Lamy J., Weill J., and Lamy J.N. A refined quaternary structure of Androctonus australis hemocyanin. Eur. J. Biochem. 127 (1982) 501-506
    • (1982) Eur. J. Biochem. , vol.127 , pp. 501-506
    • Sizaret, P.-Y.1    Frank, J.2    Lamy, J.3    Weill, J.4    Lamy, J.N.5
  • 26
    • 0023904186 scopus 로고
    • Intramoelcular localization of epitopes within an oligomeric protein by immunoelectron microscopy and image processing
    • Boisset N., Frank J., Taveau J.-C., Billiald P., Motta G., Lamy J., et al. Intramoelcular localization of epitopes within an oligomeric protein by immunoelectron microscopy and image processing. Proteins: Struct. Funct. Genet. 3 (1988) 161-183
    • (1988) Proteins: Struct. Funct. Genet. , vol.3 , pp. 161-183
    • Boisset, N.1    Frank, J.2    Taveau, J.-C.3    Billiald, P.4    Motta, G.5    Lamy, J.6
  • 28
    • 0020012273 scopus 로고
    • Hemocyanin in spiders, XV. The role of individual subunits in the assembly of Eurypelma hemocyanin
    • Markl J., Decker H., and Linzen B. Hemocyanin in spiders, XV. The role of individual subunits in the assembly of Eurypelma hemocyanin. Biol. Chem. Hoppe-Seyler 363 (1982) 73-87
    • (1982) Biol. Chem. Hoppe-Seyler , vol.363 , pp. 73-87
    • Markl, J.1    Decker, H.2    Linzen, B.3
  • 29
    • 0034671529 scopus 로고    scopus 로고
    • Complete sequence of the 24-mer hemocyanin of the tarantula Eurypelma californicum
    • Voit R., Feldmaier-Fuchs G., Schweikardt T., Decker H., and Burmester T. Complete sequence of the 24-mer hemocyanin of the tarantula Eurypelma californicum. J. Biol. Chem. 275 (2000) 39339-39344
    • (2000) J. Biol. Chem. , vol.275 , pp. 39339-39344
    • Voit, R.1    Feldmaier-Fuchs, G.2    Schweikardt, T.3    Decker, H.4    Burmester, T.5
  • 30
    • 0037177839 scopus 로고    scopus 로고
    • Complete hemocyanin-subunit sequences of the hunting spider Cupiennius salei: recent hemocyanin-remodelling in entelegyne spiders
    • Ballweber P., Markl J., and Burmester T. Complete hemocyanin-subunit sequences of the hunting spider Cupiennius salei: recent hemocyanin-remodelling in entelegyne spiders. J. Biol. Chem. 277 (2002) 14451-14457
    • (2002) J. Biol. Chem. , vol.277 , pp. 14451-14457
    • Ballweber, P.1    Markl, J.2    Burmester, T.3
  • 31
    • 0042427754 scopus 로고    scopus 로고
    • Subunit sequences of the 4x6-mer hemocyanin from the golden orb-web spider Nephila inaurata: intramolecular evolution of the chelicerate hemocyanin subunits
    • Averdam A., Markl J., and Burmester T. Subunit sequences of the 4x6-mer hemocyanin from the golden orb-web spider Nephila inaurata: intramolecular evolution of the chelicerate hemocyanin subunits. Eur. J. Biochem. 270 (2003) 3432-3439
    • (2003) Eur. J. Biochem. , vol.270 , pp. 3432-3439
    • Averdam, A.1    Markl, J.2    Burmester, T.3
  • 32
    • 0019728717 scopus 로고
    • Use of multivariate statistics in analysing the images of biological macromolecules
    • van Heel M., and Frank J. Use of multivariate statistics in analysing the images of biological macromolecules. Ultramicroscopy 6 (1981) 187-194
    • (1981) Ultramicroscopy , vol.6 , pp. 187-194
    • van Heel, M.1    Frank, J.2
  • 34
    • 0000284121 scopus 로고
    • Quaternary structure of multimeric arthropod hemocyanins
    • van Heel M., and Dube P. Quaternary structure of multimeric arthropod hemocyanins. Micron 25 (1994) 387-418
    • (1994) Micron , vol.25 , pp. 387-418
    • van Heel, M.1    Dube, P.2
  • 35
    • 0028237034 scopus 로고
    • The interhexameric contacts in the four-hexameric hemocyanin from the tarantula Eurypelma californicum: a tentative mechanism for cooperative behavior
    • de Haas F., and van Bruggen E.F.J. The interhexameric contacts in the four-hexameric hemocyanin from the tarantula Eurypelma californicum: a tentative mechanism for cooperative behavior. J. Mol. Biol. 237 (1994) 464-478
    • (1994) J. Mol. Biol. , vol.237 , pp. 464-478
    • de Haas, F.1    van Bruggen, E.F.J.2
  • 36
    • 0037121459 scopus 로고    scopus 로고
    • All hierarchical levels are involved in conformational transitions of the 4x6-meric tarantula hemocyanin upon oxygenation
    • Hartmann H., and Decker H. All hierarchical levels are involved in conformational transitions of the 4x6-meric tarantula hemocyanin upon oxygenation. Biochim. Biophys. Acta 1601 (2002) 132-137
    • (2002) Biochim. Biophys. Acta , vol.1601 , pp. 132-137
    • Hartmann, H.1    Decker, H.2
  • 37
    • 0028832525 scopus 로고
    • Three-dimensional reconstruction of Androctonus australis hemocyanin labelled with a monoclonal Fab fragment
    • Boisset N., Penczek P., Taveau J.-C., Lamy J., Frank J., and Lamy J. Three-dimensional reconstruction of Androctonus australis hemocyanin labelled with a monoclonal Fab fragment. J. Struct. Biol. 115 (1995) 16-29
    • (1995) J. Struct. Biol. , vol.115 , pp. 16-29
    • Boisset, N.1    Penczek, P.2    Taveau, J.-C.3    Lamy, J.4    Frank, J.5    Lamy, J.6
  • 38
    • 0031567107 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of Limulus polyphemus hemocyanin from cryoelectron microscopy
    • Taveau J.-C., Boisset N., Lamy J., Lambert O., and Lamy J.N. Three-dimensional reconstruction of Limulus polyphemus hemocyanin from cryoelectron microscopy. J. Mol. Biol. 266 (1997) 1002-1015
    • (1997) J. Mol. Biol. , vol.266 , pp. 1002-1015
    • Taveau, J.-C.1    Boisset, N.2    Lamy, J.3    Lambert, O.4    Lamy, J.N.5
  • 39
    • 0037255448 scopus 로고    scopus 로고
    • Quaternary structure of the European spiny lobster (Palinurus elephas) 1x6-mer hemocyanin from cryoEM and amino acid sequence data
    • Meissner U., Stohr M., Kusche K., Burmester T., Stark H., Harris J.R., et al. Quaternary structure of the European spiny lobster (Palinurus elephas) 1x6-mer hemocyanin from cryoEM and amino acid sequence data. J. Mol. Biol. 325 (2003) 99-109
    • (2003) J. Mol. Biol. , vol.325 , pp. 99-109
    • Meissner, U.1    Stohr, M.2    Kusche, K.3    Burmester, T.4    Stark, H.5    Harris, J.R.6
  • 41
    • 0021113922 scopus 로고
    • Assembly and calcium-dependent cooperativity of Limulus IV hemocyanin: a model system for analysis of structure-function relationships in the absence of subunit heterogeneity
    • Brenowitz M., Bonaventura C., and Bonaventura J. Assembly and calcium-dependent cooperativity of Limulus IV hemocyanin: a model system for analysis of structure-function relationships in the absence of subunit heterogeneity. Biochemistry 22 (1983) 4707-4713
    • (1983) Biochemistry , vol.22 , pp. 4707-4713
    • Brenowitz, M.1    Bonaventura, C.2    Bonaventura, J.3
  • 42
    • 0024293432 scopus 로고
    • Hemocyanins in spiders, XXII. Range of allosteric interaction in a four-hexamer hemocyanin: co-operativity and Bohr effect of dissociation intermediates
    • Savel-Niemann A., Markl J., and Linzen B. Hemocyanins in spiders, XXII. Range of allosteric interaction in a four-hexamer hemocyanin: co-operativity and Bohr effect of dissociation intermediates. J. Mol. Biol. 204 (1988) 385-395
    • (1988) J. Mol. Biol. , vol.204 , pp. 385-395
    • Savel-Niemann, A.1    Markl, J.2    Linzen, B.3
  • 43
    • 0024982116 scopus 로고
    • Allosteric control in Limulus polyphemus hemocyanin: functional relevance of interactions between hexamers
    • Brouwer, and Serigstad. Allosteric control in Limulus polyphemus hemocyanin: functional relevance of interactions between hexamers. Biochemistry. 28 (1989) 8819-8827
    • (1989) Biochemistry. , vol.28 , pp. 8819-8827
    • Brouwer1    Serigstad2
  • 46
    • 0036297629 scopus 로고    scopus 로고
    • Multi-resolution contour-based fitting of macromolecular structures
    • Chacón P., and Wriggers W. Multi-resolution contour-based fitting of macromolecular structures. J. Mol. Biol. 317 (2002) 375-384
    • (2002) J. Mol. Biol. , vol.317 , pp. 375-384
    • Chacón, P.1    Wriggers, W.2
  • 47
    • 0018639079 scopus 로고
    • Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease
    • Chirgwin J.M., Przbyla A.E., MacDonald R.J., and Rutter W.J. Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry 18 (1979) 5294-5299
    • (1979) Biochemistry , vol.18 , pp. 5294-5299
    • Chirgwin, J.M.1    Przbyla, A.E.2    MacDonald, R.J.3    Rutter, W.J.4
  • 48
    • 0034849408 scopus 로고    scopus 로고
    • MRBAYES: Bayesian inference of phylogenetic trees
    • Huelsenbeck J.P., and Ronquist F. MRBAYES: Bayesian inference of phylogenetic trees. Bioinformatics 17 (2001) 754-755
    • (2001) Bioinformatics , vol.17 , pp. 754-755
    • Huelsenbeck, J.P.1    Ronquist, F.2
  • 49
    • 0035031966 scopus 로고    scopus 로고
    • A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach
    • Whelan S., and Goldman N. A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach. Mol. Biol. Evol. 18 (2001) 691-699
    • (2001) Mol. Biol. Evol. , vol.18 , pp. 691-699
    • Whelan, S.1    Goldman, N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.