메뉴 건너뛰기




Volumn 273, Issue 2, 1997, Pages 479-500

Charges, hydrogen bonds, and correlated motions in the 1 Å resolution refined structure of the mating pheromone Er-1 from Euplotes raikovi

Author keywords

Anisotropy; Atomic resolution; Helix caps; Hydrogen bonds; Pheromone

Indexed keywords

ALCOHOL; AMINO ACID; HYDROGEN; PHEROMONE; WATER;

EID: 0030781412     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1318     Document Type: Article
Times cited : (10)

References (48)
  • 1
    • 0000342517 scopus 로고    scopus 로고
    • A challenging case for protein crystal structure determination: The mating pheromone ErEuplotes raikovi
    • Anderson D. H., Weiss M. S., Eisenberg D. A challenging case for protein crystal structure determination: the mating pheromone ErEuplotes raikovi. Acta Crystallog. sect. D. 52:1996;469-480.
    • (1996) Acta Crystallog. Sect. D , vol.52 , pp. 469-480
    • Anderson, D.H.1    Weiss, M.S.2    Eisenberg, D.3
  • 4
    • 0023643147 scopus 로고
    • The high-resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leechHirudo medicinalis
    • Bode W., Papamokos E., Musil D. The high-resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leechHirudo medicinalis. Eur. J. Biochem. 166:1987;673-692.
    • (1987) Eur. J. Biochem. , vol.166 , pp. 673-692
    • Bode, W.1    Papamokos, E.2    Musil, D.3
  • 10
    • 0028080176 scopus 로고
    • The third IgG-binding domain from Streptococcal protein G: An analysis by X-ray crystallography of the structure alone and in a complex with Fab
    • Derrick J. P., Wigley D. B. The third IgG-binding domain from Streptococcal protein G: an analysis by X-ray crystallography of the structure alone and in a complex with Fab. J. Mol. Biol. 243:1994;906-918.
    • (1994) J. Mol. Biol. , vol.243 , pp. 906-918
    • Derrick, J.P.1    Wigley, D.B.2
  • 11
    • 0000568418 scopus 로고
    • RESTRAIN: Restrained structure-factor least-squares refinement program for macromolecular structures
    • Driessen H., Haneef M. I. J., Harris G. W., Howlin B., Khan G., Moss D. S. RESTRAIN: restrained structure-factor least-squares refinement program for macromolecular structures. J. Appl. Crystallog. 22:1989;510-516.
    • (1989) J. Appl. Crystallog. , vol.22 , pp. 510-516
    • Driessen, H.1    Haneef, M.I.J.2    Harris, G.W.3    Howlin, B.4    Khan, G.5    Moss, D.S.6
  • 13
    • 79952608525 scopus 로고
    • Accurate bond length and angle parameters for X-ray protein-structure refinement
    • Engh R. A., Huber R. Accurate bond length and angle parameters for X-ray protein-structure refinement. Acta Crystallog. sect. A. 47:1991;392-400.
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 15
    • 0029775108 scopus 로고    scopus 로고
    • Three-dimensional structure of the α-conotoxin GI at 1. 2 Å resolution
    • Guddat L. W., Martin J. L., Edmunson A. B., Gray W. R. Three-dimensional structure of the α-conotoxin GI at 1. 2 Å resolution. Biochemistry. 35:1996;11329-11335.
    • (1996) Biochemistry , vol.35 , pp. 11329-11335
    • Guddat, L.W.1    Martin, J.L.2    Edmunson, A.B.3    Gray, W.R.4
  • 16
    • 0030584684 scopus 로고    scopus 로고
    • The 1.1 Å crystal structure of the neuronal acetylcholine receptor antagonist, α-conotoxin PnIA fromConus pennaceus
    • Hu S-H., Gehrmann J., Guddat L. W., Alewood P. F., Craik D. J., Martin J. L. The 1.1 Å crystal structure of the neuronal acetylcholine receptor antagonist, α-conotoxin PnIA fromConus pennaceus. Structure. 4:1996;417-423.
    • (1996) Structure , vol.4 , pp. 417-423
    • Hu, S-H.1    Gehrmann, J.2    Guddat, L.W.3    Alewood, P.F.4    Craik, D.J.5    Martin, J.L.6
  • 17
    • 0001504410 scopus 로고
    • Abbreviations and symbols for the description of the conformation of polypeptide chains. Tentative rules (1969)
    • M. Abbreviations and symbols for the description of the conformation of polypeptide chains. Tentative rules (1969). J. Biol. Chem. 245:1970;6489-6497.
    • (1970) J. Biol. Chem. , vol.245 , pp. 6489-6497
  • 18
    • 84988072575 scopus 로고
    • Abbreviations and symbols for the description of conformations of polynucleotide chains
    • M. Abbreviations and symbols for the description of conformations of polynucleotide chains. Eur. J. Biochem. 131:1983;9-15.
    • (1983) Eur. J. Biochem. , vol.131 , pp. 9-15
  • 20
    • 0030513191 scopus 로고    scopus 로고
    • An eye lens protein-water structure: 1.2 Å resolution structure of γb-crystallin at 150 K
    • Kumaraswamy V. S., Lindley P. F., Slingsby C., Glover I. D. An eye lens protein-water structure: 1.2 Å resolution structure of γB-crystallin at 150 K. Acta Crystallog. sect. D. 52:1996;611-622.
    • (1996) Acta Crystallog. Sect. D , vol.52 , pp. 611-622
    • Kumaraswamy, V.S.1    Lindley, P.F.2    Slingsby, C.3    Glover, I.D.4
  • 21
    • 0024281641 scopus 로고
    • Three-dimensional structure at 0.86 Å of the uncomplexed form of the transmembrane ion channel peptide gramicidin A
    • Langs D. A. Three-dimensional structure at 0.86 Å of the uncomplexed form of the transmembrane ion channel peptide gramicidin A. Science. 241:1988;188-191.
    • (1988) Science , vol.241 , pp. 188-191
    • Langs, D.A.1
  • 22
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski R. A., MacArthur M. W., Moss D. S., Thornton J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;283-291.
    • (1993) J. Appl. Crystallog , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 24
    • 0001099937 scopus 로고
    • Traitment statistique des erreurs dans la détermination des structures cristallines
    • Luzzati V. Traitment statistique des erreurs dans la détermination des structures cristallines. Acta Crystallog. 5:1952;802-810.
    • (1952) Acta Crystallog. , vol.5 , pp. 802-810
    • Luzzati, V.1
  • 27
    • 84987486517 scopus 로고
    • Competition among homologous polypeptide pheromones of the ciliateEuplotes raikovi
    • Ortenzi C., Luporini P. Competition among homologous polypeptide pheromones of the ciliateEuplotes raikovi. J. Eukaryotic Microbiol. 42:1995;242-248.
    • (1995) J. Eukaryotic Microbiol. , vol.42 , pp. 242-248
    • Ortenzi, C.1    Luporini, P.2
  • 30
    • 0030000448 scopus 로고    scopus 로고
    • π-Turns in proteins and peptides: Classification, conformation, occurrence, hydration and sequence
    • Rajashankar K. R., Ramakumar S. π-Turns in proteins and peptides: classification, conformation, occurrence, hydration and sequence. Protein Sci. 5:1996;932-946.
    • (1996) Protein Sci. , vol.5 , pp. 932-946
    • Rajashankar, K.R.1    Ramakumar, S.2
  • 33
    • 0028168922 scopus 로고
    • Structural characteristics for biological activity of heat-stable enterotoxin produced by enterotoxigenicEscherichia coli
    • Sato T., Ozaki H., Hata Y., Kitagawa Y., Katsube Y., Shimonishi Y. Structural characteristics for biological activity of heat-stable enterotoxin produced by enterotoxigenicEscherichia coli. Biochemistry. 33:1994;8641-8650.
    • (1994) Biochemistry , vol.33 , pp. 8641-8650
    • Sato, T.1    Ozaki, H.2    Hata, Y.3    Kitagawa, Y.4    Katsube, Y.5    Shimonishi, Y.6
  • 34
    • 0026712235 scopus 로고
    • Refinement of the structure of recombinant rat intestinal fatty acid-binding apoprotein at 1.2 Å resolution
    • Scapin G., Gordon J. I., Sacchettini J. C. Refinement of the structure of recombinant rat intestinal fatty acid-binding apoprotein at 1.2 Å resolution. J. Biol. Chem. 267:1992;4253-4269.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4253-4269
    • Scapin, G.1    Gordon, J.I.2    Sacchettini, J.C.3
  • 35
    • 0027293405 scopus 로고
    • Complex of ribonuclease Sa with a cyclic nucleotide and a proposed model for the reaction intermediate
    • Sevcik J., Dauter Z., Lamzin V. S., Wilson K. S. Complex of ribonuclease Sa with a cyclic nucleotide and a proposed model for the reaction intermediate. Eur. J. Biochem. 216:1993;301-305.
    • (1993) Eur. J. Biochem. , vol.216 , pp. 301-305
    • Sevcik, J.1    Dauter, Z.2    Lamzin, V.S.3    Wilson, K.S.4
  • 37
    • 0001841380 scopus 로고
    • On the rigid body motion of molecules in crystals
    • Shomaker V., Trueblood K. N. On the rigid body motion of molecules in crystals. Acta Crystallog. sect. B. 24:1968;63-74.
    • (1968) Acta Crystallog. Sect. B , vol.24 , pp. 63-74
    • Shomaker, V.1    Trueblood, K.N.2
  • 39
    • 0030471364 scopus 로고    scopus 로고
    • The role of water in sequence-independent ligand binding by an oligopeptide transporter protein
    • Tame J. R. H., Sleigh S. H., Wilkinson A. J., Ladbury J. E. The role of water in sequence-independent ligand binding by an oligopeptide transporter protein. Nature Struct. Biol. 3:1996;998-1001.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 998-1001
    • Tame, J.R.H.1    Sleigh, S.H.2    Wilkinson, A.J.3    Ladbury, J.E.4
  • 40
    • 0001554681 scopus 로고
    • Water structure of a hydrophobic protein at atomic resolution: Pentagon rings of water molecules in crystals of crambin
    • Teeter M. M. Water structure of a hydrophobic protein at atomic resolution: pentagon rings of water molecules in crystals of crambin. Proc. Natl Acad. Sci. USA. 81:1984;6014-6018.
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 6014-6018
    • Teeter, M.M.1
  • 41
    • 0027459475 scopus 로고
    • Atomic resolution (0.83 Å) crystal structure of the hydrophobic protein crambin at 130 K
    • Teeter M. M., Roe S. M., Hoe N. H. Atomic resolution (0.83 Å) crystal structure of the hydrophobic protein crambin at 130 K. J. Mol. Biol. 230:1993;292-311.
    • (1993) J. Mol. Biol. , vol.230 , pp. 292-311
    • Teeter, M.M.1    Roe, S.M.2    Hoe, N.H.3
  • 42
    • 0029967679 scopus 로고    scopus 로고
    • Crystal structures of the human p56lck SH2 domain in complex with two short phosphotyrosyl peptides at 1.0 Å and 1.8 Å resolution
    • Tong L., Warren T. C., King J., Betageri R., Rose J., Jakes S. Crystal structures of the human p56lck SH2 domain in complex with two short phosphotyrosyl peptides at 1.0 Å and 1.8 Å resolution. J. Mol. Biol. 256:1996;601-610.
    • (1996) J. Mol. Biol. , vol.256 , pp. 601-610
    • Tong, L.1    Warren, T.C.2    King, J.3    Betageri, R.4    Rose, J.5    Jakes, S.6
  • 44
    • 0029117482 scopus 로고
    • Autocrine mitogenic activity of pheromones produced by the protozoan ciliateEuplotes raikovi
    • Vallesi A., Giull G., Bradshaw R. A., Luporini P. Autocrine mitogenic activity of pheromones produced by the protozoan ciliateEuplotes raikovi. Nature. 376:1995;522-524.
    • (1995) Nature , vol.376 , pp. 522-524
    • Vallesi, A.1    Giull, G.2    Bradshaw, R.A.3    Luporini, P.4
  • 45
    • 0028800215 scopus 로고
    • A cooperative model for receptor recognition and cell adhesion: Evidence from the molecular packing in the 1. 6-Å crystal structure of the pheromone ErEuplotes raikovi
    • Weiss M. S., Anderson D. H., Raffioni S., Bradshaw R. A., Ortenzi C., Luporini P., Eisenberg D. A cooperative model for receptor recognition and cell adhesion: evidence from the molecular packing in the 1. 6-Å crystal structure of the pheromone ErEuplotes raikovi. Proc. Natl Acad. Sci. USA. 92:1995;10172-10176.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 10172-10176
    • Weiss, M.S.1    Anderson, D.H.2    Raffioni, S.3    Bradshaw, R.A.4    Ortenzi, C.5    Luporini, P.6    Eisenberg, D.7
  • 48
    • 0026646490 scopus 로고
    • Structure of scorpion toxin variant-3 at 1.2 Å resolution
    • Zhao B., Carson M., Ealick S. E., Bugg C. E. Structure of scorpion toxin variant-3 at 1.2 Å resolution. J. Mol. Biol. 227:1992;239-252.
    • (1992) J. Mol. Biol. , vol.227 , pp. 239-252
    • Zhao, B.1    Carson, M.2    Ealick, S.E.3    Bugg, C.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.