메뉴 건너뛰기




Volumn 7, Issue 3, 1997, Pages 422-427

Circular permutations of natural protein sequences: Structural evidence

Author keywords

[No Author keywords available]

Indexed keywords

BETA GLUCAN HYDROLASE; BETA GLUCOSIDASE; GLUCOSYLTRANSFERASE; LECTIN; PROTEIN; TRANSALDOLASE;

EID: 0030979555     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(97)80061-9     Document Type: Article
Times cited : (136)

References (40)
  • 2
    • 0021095334 scopus 로고
    • Circular and circularly permuted forms of bovine pancreatic trypsin inhibitor
    • Goldenberg DP, Creighton TE. Circular and circularly permuted forms of bovine pancreatic trypsin inhibitor. J Mol Biol. 165:1983;407-413.
    • (1983) J Mol Biol , vol.165 , pp. 407-413
    • Goldenberg, D.P.1    Creighton, T.E.2
  • 3
    • 0024490818 scopus 로고
    • Correct folding of circularly permuted variants of a βα-barrel enzyme in vivo
    • Luger K, Hommel U, Herold M, Hofsteenge J, Kirschner K. Correct folding of circularly permuted variants of a βα-barrel enzyme in vivo. Science. 243:1989;206-210.
    • (1989) Science , vol.243 , pp. 206-210
    • Luger, K.1    Hommel, U.2    Herold, M.3    Hofsteenge, J.4    Kirschner, K.5
  • 4
    • 0029422261 scopus 로고
    • Circular permutation of polypeptide chains: Implications for protein folding and stability
    • An extensive review of engineered circular permutations and their implications for protein folding and stability. of special interest
    • Heinemann U, Hahn M. Circular permutation of polypeptide chains: implications for protein folding and stability. Prog Biophys Mol Biol. 64:1995;121-143 An extensive review of engineered circular permutations and their implications for protein folding and stability. of special interest.
    • (1995) Prog Biophys Mol Biol , vol.64 , pp. 121-143
    • Heinemann, U.1    Hahn, M.2
  • 5
    • 0028099766 scopus 로고
    • Native-like in vivo folding of a circularly permuted jellyroll protein shown by crystal structure analysis
    • Hahn M, Piotukh K, Borriss R, Heinemann U. Native-like in vivo folding of a circularly permuted jellyroll protein shown by crystal structure analysis. Proc Natl Acad Sci. 91:1994;10417-10421.
    • (1994) Proc Natl Acad Sci , vol.91 , pp. 10417-10421
    • Hahn, M.1    Piotukh, K.2    Borriss, R.3    Heinemann, U.4
  • 6
    • 0027143219 scopus 로고
    • Aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains
    • Yang YR, Schachman HK. Aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains. Proc Natl Acad Sci USA. 90:1993;1980-1984.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 1980-1984
    • Yang, Y.R.1    Schachman, H.K.2
  • 7
    • 0029859408 scopus 로고    scopus 로고
    • Random circular permutation of genes and expressed polypeptide chains: Application of the method to the catalytic chains of aspartate transcarbamoylase
    • An analysis using randomized generation of circularly permuted forms of the catalytic chains of aspartate transcarbamoylase. This study reveals a remarkable tolerance of the protein structure to circular permutations. of special interest
    • Graf R, Schachman HK. Random circular permutation of genes and expressed polypeptide chains: application of the method to the catalytic chains of aspartate transcarbamoylase. Proc Natl Acad Sci USA. 93:1996;11591-11596 An analysis using randomized generation of circularly permuted forms of the catalytic chains of aspartate transcarbamoylase. This study reveals a remarkable tolerance of the protein structure to circular permutations. of special interest.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 11591-11596
    • Graf, R.1    Schachman, H.K.2
  • 8
    • 0029135360 scopus 로고
    • Increased antitumor activity of a circularly permuted interleukin 4-toxin in mice with interleukin 4 receptor-bearing human carcinoma
    • An elegant use of circular permutations applied to IL4 in a toxin chimera to avoid steric interference in binding to the target receptor. of special interest
    • Kreitman RJ, Puri RK, Pastan I. Increased antitumor activity of a circularly permuted interleukin 4-toxin in mice with interleukin 4 receptor-bearing human carcinoma. Cancer Res. 55:1995;3357-3363 An elegant use of circular permutations applied to IL4 in a toxin chimera to avoid steric interference in binding to the target receptor. of special interest.
    • (1995) Cancer Res , vol.55 , pp. 3357-3363
    • Kreitman, R.J.1    Puri, R.K.2    Pastan, I.3
  • 9
    • 0022001083 scopus 로고
    • Polypeptide ligation occurs during post-translational modification of concanavalin A
    • Carrington DM, Auffret A, Hanke DE. Polypeptide ligation occurs during post-translational modification of concanavalin A. Nature. 313:1985;64-67.
    • (1985) Nature , vol.313 , pp. 64-67
    • Carrington, D.M.1    Auffret, A.2    Hanke, D.E.3
  • 12
    • 0016662479 scopus 로고
    • The covalent and 3-dimensional structure of concanavalin A. 4. Atomic coordinates, hydrogen bonding and quaternary structure
    • Reeke GN, Becker JW, Edelman GM. The covalent and 3-dimensional structure of concanavalin A. 4. Atomic coordinates, hydrogen bonding and quaternary structure. J Biol Chem. 250:1975;1525-1547.
    • (1975) J Biol Chem , vol.250 , pp. 1525-1547
    • Reeke, G.N.1    Becker, J.W.2    Edelman, G.M.3
  • 14
    • 0028773635 scopus 로고
    • Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain
    • Crennel S, Garman E, Laver G, Vimr E, Taylor G. Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain. Structure. 2:1994;535-544.
    • (1994) Structure , vol.2 , pp. 535-544
    • Crennel, S.1    Garman, E.2    Laver, G.3    Vimr, E.4    Taylor, G.5
  • 15
    • 0026337737 scopus 로고
    • Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose
    • Shaanan B, Lis H, Sharon N. Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose. Science. 254:1991;862-866.
    • (1991) Science , vol.254 , pp. 862-866
    • Shaanan, B.1    Lis, H.2    Sharon, N.3
  • 17
    • 0001361122 scopus 로고
    • Structure and function of genes coding for bacterial endo 1,3-1,4-β-glucanases
    • Borriss R. Structure and function of genes coding for bacterial endo 1,3-1,4-β-glucanases. Curr Top Mol Genet. 2:1994;163-188.
    • (1994) Curr Top Mol Genet , vol.2 , pp. 163-188
    • Borriss, R.1
  • 18
    • 0026569381 scopus 로고
    • Structure of the Clostridium thermocellum gene licB and the encoded β-1,3-1,4-glucanase
    • Schimming S, Schwarz WH, Staudenbauer WL. Structure of the Clostridium thermocellum gene licB and the encoded β-1,3-1,4-glucanase. Eur J Biochem. 204:1992;13-19.
    • (1992) Eur J Biochem , vol.204 , pp. 13-19
    • Schimming, S.1    Schwarz, W.H.2    Staudenbauer, W.L.3
  • 19
    • 0029360566 scopus 로고
    • Circular permutations of protein sequence: Not so rare?
    • A convincing case for the occurrence of a circular permutation in bacterial β-glucanases is made on the basis of evidence from its primary and tertiary structure. of special interest
    • Heinemann U, Hahn M. Circular permutations of protein sequence: not so rare? Trends Biochem Sci. 20:1995;349-350 A convincing case for the occurrence of a circular permutation in bacterial β-glucanases is made on the basis of evidence from its primary and tertiary structure. of special interest.
    • (1995) Trends Biochem Sci , vol.20 , pp. 349-350
    • Heinemann, U.1    Hahn, M.2
  • 20
    • 0027161796 scopus 로고
    • Molecular and active-site structure of Bacillus 1,3-1,4-β-glucanase
    • Keitel T, Simon O, Borriss R, Heinermann U. Molecular and active-site structure of Bacillus 1,3-1,4-β-glucanase. Proc Natl Acad Sci USA. 90:1993;5287-5291.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 5287-5291
    • Keitel, T.1    Simon, O.2    Borriss, R.3    Heinermann, U.4
  • 21
    • 0029000740 scopus 로고
    • Swaposins: Circular permutations within genes encoding saposin homologues
    • A domain in a barley grain aspartic protease is detected to be homologous to saposin if a circular permutation of the sequence is inferred. A probable mechanism for the formation of circular permutations is suggested. of outstanding interest
    • Ponting CP, Russell RB. Swaposins: circular permutations within genes encoding saposin homologues. Trends Biochem Sci. 20:1995;179-180 A domain in a barley grain aspartic protease is detected to be homologous to saposin if a circular permutation of the sequence is inferred. A probable mechanism for the formation of circular permutations is suggested. of outstanding interest.
    • (1995) Trends Biochem Sci , vol.20 , pp. 179-180
    • Ponting, C.P.1    Russell, R.B.2
  • 22
    • 0028108664 scopus 로고
    • Comparative modelling of barley-grain aspartic proteinase: A structural rationale for observed hydrolytic specificity
    • Guruprasad K, Tormakangas K, Kervinen J, Blundell TL. Comparative modelling of barley-grain aspartic proteinase: a structural rationale for observed hydrolytic specificity. FEBS Lett. 352:1994;131-136.
    • (1994) FEBS Lett , vol.352 , pp. 131-136
    • Guruprasad, K.1    Tormakangas, K.2    Kervinen, J.3    Blundell, T.L.4
  • 23
    • 0029671161 scopus 로고    scopus 로고
    • A circularly permuted α-amylase-type α/β-barrel structure in glucan-synthesizing glucosyltransferases
    • An example of how careful sequence comparisons can reveal circular permutations in proteins with low sequence homologies. of special interest
    • MacGregor EA, Jespersen HM, Svensson B. A circularly permuted α-amylase-type α/β-barrel structure in glucan-synthesizing glucosyltransferases. FEBS Lett. 378:1996;263-266 An example of how careful sequence comparisons can reveal circular permutations in proteins with low sequence homologies. of special interest.
    • (1996) FEBS Lett , vol.378 , pp. 263-266
    • MacGregor, E.A.1    Jespersen, H.M.2    Svensson, B.3
  • 24
  • 25
    • 0025129872 scopus 로고
    • Hydrophobic cluster analysis: Procedures to derive structural and functional information from 2-D-representation of protein sequences
    • Lemesle-Varloot L, Henrissat B, Gaboriaud C, Bissery V. Hydrophobic cluster analysis: procedures to derive structural and functional information from 2-D-representation of protein sequences. Biochimie. 72:1990;555-574.
    • (1990) Biochimie , vol.72 , pp. 555-574
    • Lemesle-Varloot, L.1    Henrissat, B.2    Gaboriaud, C.3    Bissery, V.4
  • 26
    • 0030562068 scopus 로고    scopus 로고
    • A sequence analysis of the β-glucosidase sub-family B
    • Rojas A, Romeu A. A sequence analysis of the β-glucosidase sub-family B. FEBS Lett. 378:1996;93-97.
    • (1996) FEBS Lett , vol.378 , pp. 93-97
    • Rojas, A.1    Romeu, A.2
  • 27
    • 0028262129 scopus 로고
    • Domain structure of the Acetogenium kivui surface layer revealed by electron crystallography and sequence analysis
    • Lupas A, Engelhardt H, Peters J, Santarius U, Volker S, Baumeister W. Domain structure of the Acetogenium kivui surface layer revealed by electron crystallography and sequence analysis. J Bacteriol. 176:1994;1224-1233.
    • (1994) J Bacteriol , vol.176 , pp. 1224-1233
    • Lupas, A.1    Engelhardt, H.2    Peters, J.3    Santarius, U.4    Volker, S.5    Baumeister, W.6
  • 28
    • 0029899653 scopus 로고    scopus 로고
    • A circular permutation event in the evolution of the SLH domain?
    • From multiple sequence alignment, a circular permutation event, spanning three SLH domains, is suggested for three proteins from Clostridium thermocellum. of special interest
    • Lupas A. A circular permutation event in the evolution of the SLH domain? Mol Microbiol. 20:1996;897-898 From multiple sequence alignment, a circular permutation event, spanning three SLH domains, is suggested for three proteins from Clostridium thermocellum. of special interest.
    • (1996) Mol Microbiol , vol.20 , pp. 897-898
    • Lupas, A.1
  • 29
    • 0023446039 scopus 로고
    • Molecular architecture of rabbit skeletal muscle aldolase at 2.7 Å resolution
    • Sygusch J, Beaudry D, Allaire M. Molecular architecture of rabbit skeletal muscle aldolase at 2.7 Å resolution. Proc Natl Acad Sci USA. 84:1987;7846-7850.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 7846-7850
    • Sygusch, J.1    Beaudry, D.2    Allaire, M.3
  • 31
    • 1842332171 scopus 로고    scopus 로고
    • Crystal structure of the reduced Schiff-base intermediate complex of transaldolase B from Escherichia coli: Mechanistic implications for class I aldolases
    • Jia J, Schörken U, Lindqvist Y, Sprenger GA, Schneider G. Crystal structure of the reduced Schiff-base intermediate complex of transaldolase B from Escherichia coli: mechanistic implications for class I aldolases. Protein Sci. 6:1997;1-6.
    • (1997) Protein Sci , vol.6 , pp. 1-6
    • Jia, J.1    Schörken, U.2    Lindqvist, Y.3    Sprenger, G.A.4    Schneider, G.5
  • 32
    • 0030585419 scopus 로고    scopus 로고
    • Crystal structure of transaldolase B from Escherichia coli suggests a circular permutation of the α/β barrel within the class I aldolase family
    • The crystal structure analysis of transaldolase and its comparison with the structure of other class I aldolases provides evidence that a circular permutation has occurred in this enzyme family. of outstanding interest
    • Jia J, Huang W, Schörken U, Sahm H, Sprenger GA, Lindqvist Y, Schneider G. Crystal structure of transaldolase B from Escherichia coli suggests a circular permutation of the α/β barrel within the class I aldolase family. Structure. 4:1996;715-724 The crystal structure analysis of transaldolase and its comparison with the structure of other class I aldolases provides evidence that a circular permutation has occurred in this enzyme family. of outstanding interest.
    • (1996) Structure , vol.4 , pp. 715-724
    • Jia, J.1    Huang, W.2    Schörken, U.3    Sahm, H.4    Sprenger, G.A.5    Lindqvist, Y.6    Schneider, G.7
  • 33
    • 0028773463 scopus 로고
    • The three-dimensional structure of N-acetylneuraminate lyase from Escherichia coli
    • Izard T, Lawrence MC, Malby RL, Lilley GG, Colman PM. The three-dimensional structure of N-acetylneuraminate lyase from Escherichia coli. Structure. 2:1994;361-369.
    • (1994) Structure , vol.2 , pp. 361-369
    • Izard, T.1    Lawrence, M.C.2    Malby, R.L.3    Lilley, G.G.4    Colman, P.M.5
  • 34
    • 0028907826 scopus 로고
    • The crystal structure of dihydropicolinate synthase from Escherichia coli at 2.5 Å resolution
    • Mirwaldt C, Korndsrfer I, Huber R. The crystal structure of dihydropicolinate synthase from Escherichia coli at 2.5 Å resolution. J Mol Biol. 246:1995;227-239.
    • (1995) J Mol Biol , vol.246 , pp. 227-239
    • Mirwaldt, C.1    Korndsrfer, I.2    Huber, R.3
  • 35
    • 0028986240 scopus 로고
    • 2+/phospholipid-binding fold
    • The first tertiary structure of a C2 domain is presented. of special interest
    • 2+/phospholipid-binding fold. Cell. 80:1995;929-938 The first tertiary structure of a C2 domain is presented. of special interest.
    • (1995) Cell , vol.80 , pp. 929-938
    • Sutton, R.B.1    Davletov, B.A.2    Berghuis, A.M.3    Sÿdhof, T.C.4    Sprang, S.R.5
  • 36
    • 0029924329 scopus 로고    scopus 로고
    • Crystal structure of a mammalian phosphoinositide-specific phospholipase Cδ
    • A comparison of the C2 domain of mammalian phosphoinositide - specific phospholipase Cδ with that from synaptogamin I reveals that they are topologically distinct but related by a circular permutation. of special interest
    • Essen L-O, Perisic O, Katan M, Williams RL. Crystal structure of a mammalian phosphoinositide-specific phospholipase Cδ Nature. 380:1996;595-602 A comparison of the C2 domain of mammalian phosphoinositide - specific phospholipase Cδ with that from synaptogamin I reveals that they are topologically distinct but related by a circular permutation. of special interest.
    • (1996) Nature , vol.380 , pp. 595-602
    • Essen, L.-O.1    Perisic, O.2    Katan, M.3    Williams, R.L.4
  • 37
    • 0030467967 scopus 로고    scopus 로고
    • The C2 domain calcium-binding motif: Structural and functional diversity
    • Amino acid sequence comparisons of 65 C2 domains show that they can be divided into two classes corresponding to the two distinct topologies found and provide evidence that these have arisen by a circular permutation. of outstanding interest
    • Nalefski EA, Falke JJ. The C2 domain calcium-binding motif: structural and functional diversity. Protein Sci. 5:1996;2375-2390 Amino acid sequence comparisons of 65 C2 domains show that they can be divided into two classes corresponding to the two distinct topologies found and provide evidence that these have arisen by a circular permutation. of outstanding interest.
    • (1996) Protein Sci , vol.5 , pp. 2375-2390
    • Nalefski, E.A.1    Falke, J.J.2
  • 38
    • 0020520185 scopus 로고
    • Amino and carboxy-terminal regions in globular proteins
    • Thornton JM, Sibanda BL. Amino and carboxy-terminal regions in globular proteins. J Mol Biol. 167:1983;443-460.
    • (1983) J Mol Biol , vol.167 , pp. 443-460
    • Thornton, J.M.1    Sibanda, B.L.2
  • 40
    • 0028052114 scopus 로고
    • 8 proteins using hydrogen bonding pattern
    • 8 proteins using hydrogen bonding pattern. J Mol Biol. 244:1994;168-182.
    • (1994) J Mol Biol , vol.244 , pp. 168-182
    • Sergeev, Y.1    Lee, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.