메뉴 건너뛰기




Volumn 73, Issue 1, 2008, Pages 113-125

Structure of the partially unliganded met state of 400 kDa hemoglobin: Insights into ligand-induced structural changes of giant hemoglobins

Author keywords

Annelida; Crystal structure; Hemoglobin; Polychaete; Unliganded

Indexed keywords

HEMOGLOBIN; LIGAND; PROTEIN SUBUNIT;

EID: 50849127885     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22040     Document Type: Article
Times cited : (6)

References (40)
  • 2
    • 0035336687 scopus 로고    scopus 로고
    • Cooperative hemoglobins: Conserved fold, diverse quaternary assemblies and allosteric mechanisms
    • Royer WE, Jr, Knapp JE, Strand K, Heaslet HA. Cooperative hemoglobins: conserved fold, diverse quaternary assemblies and allosteric mechanisms. Trends Biochem Sci 2001;26:297-304.
    • (2001) Trends Biochem Sci , vol.26 , pp. 297-304
    • Royer Jr, W.E.1    Knapp, J.E.2    Strand, K.3    Heaslet, H.A.4
  • 4
    • 0035066385 scopus 로고    scopus 로고
    • Nonvertebrate hemoglobins: Functions and molecular adaptations
    • Weber RE, Vinogradov SN. Nonvertebrate hemoglobins: functions and molecular adaptations. Physiol Rev 2001;81:569-628.
    • (2001) Physiol Rev , vol.81 , pp. 569-628
    • Weber, R.E.1    Vinogradov, S.N.2
  • 5
    • 0029882788 scopus 로고    scopus 로고
    • The multi-hemoglobin system of the hydrothermal vent tube worm Riftia pachyptila. II. Complete polypeptide chain composition investigated by maximum entropy analysis of mass spectra
    • Zal F, Lallier FH, Green BN, Vinogradov SN, Toulmond A. The multi-hemoglobin system of the hydrothermal vent tube worm Riftia pachyptila. II. Complete polypeptide chain composition investigated by maximum entropy analysis of mass spectra. J Biol Chem 1996;271:8875-8881.
    • (1996) J Biol Chem , vol.271 , pp. 8875-8881
    • Zal, F.1    Lallier, F.H.2    Green, B.N.3    Vinogradov, S.N.4    Toulmond, A.5
  • 6
    • 18144380337 scopus 로고    scopus 로고
    • Purification, characterization and sequence analyses of the extracellular giant hemoglobin from Oligobrachia mashikoi
    • Nakagawa T, Onoda S, Kanemori M, Sasayama Y, Fukumori Y. Purification, characterization and sequence analyses of the extracellular giant hemoglobin from Oligobrachia mashikoi. Zoolog Sci 2005;22: 283-291.
    • (2005) Zoolog Sci , vol.22 , pp. 283-291
    • Nakagawa, T.1    Onoda, S.2    Kanemori, M.3    Sasayama, Y.4    Fukumori, Y.5
  • 7
    • 0042844884 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometric composition of the 400 kDa hemoglobin from the pogonophoran Oligobrachia mashikoi and the primary structures of three major globin chains
    • Yuasa HJ, Green BN, Takagi T, Suzuki N, Vinogradov SN, Suzuki T. Electrospray ionization mass spectrometric composition of the 400 kDa hemoglobin from the pogonophoran Oligobrachia mashikoi and the primary structures of three major globin chains. Biochim Biophys Acta 1996;1296:235-244.
    • (1996) Biochim Biophys Acta , vol.1296 , pp. 235-244
    • Yuasa, H.J.1    Green, B.N.2    Takagi, T.3    Suzuki, N.4    Vinogradov, S.N.5    Suzuki, T.6
  • 8
    • 33846363872 scopus 로고    scopus 로고
    • Adaptations to hypoxia in hydrothermal-vent and cold-seep invertebrates
    • Hourdez S, Lallier FH. Adaptations to hypoxia in hydrothermal-vent and cold-seep invertebrates. Rev Environ Sci Biotechnol 2007; 6:143-159.
    • (2007) Rev Environ Sci Biotechnol , vol.6 , pp. 143-159
    • Hourdez, S.1    Lallier, F.H.2
  • 9
    • 0000692741 scopus 로고
    • The sulphide-binding protein in the blood of the vestimentiferan tube-worm. Riftia pachyptila, is the extracellular haemoglobin
    • Arp AJ, Childress JJ, Vetter RD. The sulphide-binding protein in the blood of the vestimentiferan tube-worm. Riftia pachyptila, is the extracellular haemoglobin. J Exp Biol 1987;128:139-158.
    • (1987) J Exp Biol , vol.128 , pp. 139-158
    • Arp, A.J.1    Childress, J.J.2    Vetter, R.D.3
  • 10
    • 26844478173 scopus 로고    scopus 로고
    • Structure of an extracellular giant hemoglobin of the gutless beard worm Oligobrachia mashikoi
    • Numoto N, Nakagawa T, Kita A, Sasayama Y, Fukumori Y, Miki K. Structure of an extracellular giant hemoglobin of the gutless beard worm Oligobrachia mashikoi. Proc Natl Acad Sci USA 2005;102: 14521-14526.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 14521-14526
    • Numoto, N.1    Nakagawa, T.2    Kita, A.3    Sasayama, Y.4    Fukumori, Y.5    Miki, K.6
  • 12
  • 13
    • 33745843278 scopus 로고    scopus 로고
    • Lumbricus erythrocruorin at 3.5 A resolution: Architecture of a megadalton respiratory complex
    • Royer WE, Jr, Sharma H, Strand K, Knapp JE, Bhyravbhatla B. Lumbricus erythrocruorin at 3.5 A resolution: architecture of a megadalton respiratory complex. Structure 2006;14:1167-1177.
    • (2006) Structure , vol.14 , pp. 1167-1177
    • Royer Jr, W.E.1    Sharma, H.2    Strand, K.3    Knapp, J.E.4    Bhyravbhatla, B.5
  • 14
    • 7044270825 scopus 로고    scopus 로고
    • Crystal structure of the hemoglobin dodecamer from Lumbricus erythrocruorin: Allosteric core of giant annelid respiratory complexes
    • Strand K, Knapp JE, Bhyravbhatla B, Royer WE, Jr. Crystal structure of the hemoglobin dodecamer from Lumbricus erythrocruorin: allosteric core of giant annelid respiratory complexes. J Mol Biol 2004;344:119-134.
    • (2004) J Mol Biol , vol.344 , pp. 119-134
    • Strand, K.1    Knapp, J.E.2    Bhyravbhatla, B.3    Royer Jr., W.E.4
  • 15
    • 33751419009 scopus 로고    scopus 로고
    • Low resolution crystal structure of Arenicola erythrocruorin: Influence of coiled coils on the architecture of a megadalton respiratory protein
    • Royer WE, Jr, Omartian MN, Knapp JE. Low resolution crystal structure of Arenicola erythrocruorin: influence of coiled coils on the architecture of a megadalton respiratory protein. J Mol Biol 2007; 365:226-236.
    • (2007) J Mol Biol , vol.365 , pp. 226-236
    • Royer Jr, W.E.1    Omartian, M.N.2    Knapp, J.E.3
  • 16
    • 0029146246 scopus 로고
    • Structural analysis of monomeric hemichrome and dimeric cyanomet hemoglobins from Caudina arenicola
    • Mitchell DT, Kitto GB, Hackert ML. Structural analysis of monomeric hemichrome and dimeric cyanomet hemoglobins from Caudina arenicola. J Mol Biol 1995;251:421-431.
    • (1995) J Mol Biol , vol.251 , pp. 421-431
    • Mitchell, D.T.1    Kitto, G.B.2    Hackert, M.L.3
  • 17
    • 0028009317 scopus 로고
    • High-resolution crystallographic analysis of a cooperative dimeric hemoglobin
    • Royer WE, Jr. High-resolution crystallographic analysis of a cooperative dimeric hemoglobin. J Mol Biol 1994;235:657-681.
    • (1994) J Mol Biol , vol.235 , pp. 657-681
    • Royer Jr., W.E.1
  • 18
    • 0028896548 scopus 로고
    • The 2.0 Å crystal structure of Scapharca tetrameric hemoglobin: Cooperative dimers within an allosteric tetramer
    • Royer WE, Jr, Heard KS, Harrington DJ, Chiancone E. The 2.0 Å crystal structure of Scapharca tetrameric hemoglobin: cooperative dimers within an allosteric tetramer. J Mol Biol 1995;253:168-186.
    • (1995) J Mol Biol , vol.253 , pp. 168-186
    • Royer Jr, W.E.1    Heard, K.S.2    Harrington, D.J.3    Chiancone, E.4
  • 19
    • 27644499055 scopus 로고    scopus 로고
    • Residue F4 plays a key role in modulating oxygen affinity and cooperativity in Scapharca dimeric hemoglobin
    • Knapp JE, Bonham MA, Gibson QH, Nichols JC, Royer WE, Jr. Residue F4 plays a key role in modulating oxygen affinity and cooperativity in Scapharca dimeric hemoglobin. Biochemistry 2005; 44:14419-14430.
    • (2005) Biochemistry , vol.44 , pp. 14419-14430
    • Knapp, J.E.1    Bonham, M.A.2    Gibson, Q.H.3    Nichols, J.C.4    Royer Jr., W.E.5
  • 20
    • 33646755415 scopus 로고    scopus 로고
    • Allosteric action in real time: Time-resolved crystallographic studies of a cooperative dimeric hemoglobin
    • Knapp JE, Pahl R, Srajer V, Royer WE, Jr. Allosteric action in real time: time-resolved crystallographic studies of a cooperative dimeric hemoglobin. Proc Natl Acad Sci USA 2006;103:7649-7654.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 7649-7654
    • Knapp, J.E.1    Pahl, R.2    Srajer, V.3    Royer Jr., W.E.4
  • 21
    • 0035846570 scopus 로고    scopus 로고
    • Restricting the ligand-linked heme movement in Scapharca dimeric hemoglobin reveals tight coupling between distal and proximal contributions to cooperativity
    • Knapp JE, Gibson QH, Cushing L, Royer WE, Jr. Restricting the ligand-linked heme movement in Scapharca dimeric hemoglobin reveals tight coupling between distal and proximal contributions to cooperativity. Biochemistry 2001;40:14795-14805.
    • (2001) Biochemistry , vol.40 , pp. 14795-14805
    • Knapp, J.E.1    Gibson, Q.H.2    Cushing, L.3    Royer Jr., W.E.4
  • 22
    • 0030612725 scopus 로고    scopus 로고
    • Mutation of residue Phe97 to Leu disrupts the central allosteric pathway in Scapharca dimeric hemoglobin
    • Pardanani A, Gibson QH, Colotti G, Royer WE, Jr. Mutation of residue Phe97 to Leu disrupts the central allosteric pathway in Scapharca dimeric hemoglobin. J Biol Chem 1997;272:13171-13179.
    • (1997) J Biol Chem , vol.272 , pp. 13171-13179
    • Pardanani, A.1    Gibson, Q.H.2    Colotti, G.3    Royer Jr., W.E.4
  • 24
    • 0842332876 scopus 로고    scopus 로고
    • External morphology of the posterior end, the "opisthosoma" , of the beard worm Oligobrachia mashikoi (Pogonophora)
    • Sasayama Y, Matada M, Fukumori Y, Umebayashi M, Matsuno A, Nakagawa T, Imajima M. External morphology of the posterior end, the "opisthosoma" , of the beard worm Oligobrachia mashikoi (Pogonophora). Zool Sci 2003;20:1411-1416.
    • (2003) Zool Sci , vol.20 , pp. 1411-1416
    • Sasayama, Y.1    Matada, M.2    Fukumori, Y.3    Umebayashi, M.4    Matsuno, A.5    Nakagawa, T.6    Imajima, M.7
  • 25
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 1997;276:307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 26
    • 0028103275 scopus 로고
    • Number 4. The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 1994;50:760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 27
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin A, Teplyakov A. MOLREP: an automated program for molecular replacement. J Appl Crystallogr 1997;30:1022-1025.
    • (1997) J Appl Crystallogr , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 28
    • 33644872571 scopus 로고    scopus 로고
    • LAFIRE: Software for automating the refinement process of protein-structure analysis
    • Yao M, Zhou Y, Tanaka I. LAFIRE: software for automating the refinement process of protein-structure analysis. Acta Crystallogr D Biol Crystallogr 2006;62:189-196.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 189-196
    • Yao, M.1    Zhou, Y.2    Tanaka, I.3
  • 29
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 1991;47:110-119.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 31
  • 33
    • 20644455116 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of extracellular giant hemoglobin from pogonophoran Oligobrachia mashikoi
    • Numoto N, Nakagawa T, Kita A, Sasayama Y, Fukumori Y, Miki K. Crystallization and preliminary X-ray crystallographic analysis of extracellular giant hemoglobin from pogonophoran Oligobrachia mashikoi. Biochim Biophys Acta 2005;1750:173-176.
    • (2005) Biochim Biophys Acta , vol.1750 , pp. 173-176
    • Numoto, N.1    Nakagawa, T.2    Kita, A.3    Sasayama, Y.4    Fukumori, Y.5    Miki, K.6
  • 34
    • 33745285726 scopus 로고    scopus 로고
    • The multigenic family of the extracellular hemoglobin from the annelid polychaete Arenicola marina
    • Chabasse C, Bailly X, Rousselot M, Zal F. The multigenic family of the extracellular hemoglobin from the annelid polychaete Arenicola marina. Comp Biochem Physiol B Biochem Mol Biol 2006;144:319-325.
    • (2006) Comp Biochem Physiol B Biochem Mol Biol , vol.144 , pp. 319-325
    • Chabasse, C.1    Bailly, X.2    Rousselot, M.3    Zal, F.4
  • 35
    • 0014958182 scopus 로고
    • Stereochemistry of cooperative effects in haemoglobin
    • Perutz MF. Stereochemistry of cooperative effects in haemoglobin. Nature 1970;228:726-739.
    • (1970) Nature , vol.228 , pp. 726-739
    • Perutz, M.F.1
  • 36
    • 0016824616 scopus 로고
    • Structure of deoxyhemoglobin A crystals grown from polyethylene glycol solutions
    • Ward KB, Wishner BC, Lattman EE, Love WE. Structure of deoxyhemoglobin A crystals grown from polyethylene glycol solutions. J Mol Biol 1975;98:161-177.
    • (1975) J Mol Biol , vol.98 , pp. 161-177
    • Ward, K.B.1    Wishner, B.C.2    Lattman, E.E.3    Love, W.E.4
  • 38
    • 0020173901 scopus 로고
    • Electronic distributions within protein phenylalanine aromatic rings are reflected by the three-dimensional oxygen atom environments
    • Thomas KA, Smith GM, Thomas TB, Feldmann RJ. Electronic distributions within protein phenylalanine aromatic rings are reflected by the three-dimensional oxygen atom environments. Proc Natl Acad Sci USA 1982;79:4843-4847.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 4843-4847
    • Thomas, K.A.1    Smith, G.M.2    Thomas, T.B.3    Feldmann, R.J.4
  • 40
    • 0035854658 scopus 로고    scopus 로고
    • Crystalline ligand transitions in lamprey hemoglobin. Structural evidence for the regulation of oxygen affinity
    • Heaslet HA, Royer WE, Jr. Crystalline ligand transitions in lamprey hemoglobin. Structural evidence for the regulation of oxygen affinity. J Biol Chem 2001;276:26230-26236.
    • (2001) J Biol Chem , vol.276 , pp. 26230-26236
    • Heaslet, H.A.1    Royer Jr., W.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.