메뉴 건너뛰기




Volumn 8, Issue 3, 1998, Pages 380-387

How far divergent evolution goes in proteins

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYPEPTIDASE G2; IRON SULFUR PROTEIN; PROTEINASE; STEROID DELTA ISOMERASE; THROMBIN INHIBITOR;

EID: 0032104477     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(98)80073-0     Document Type: Article
Times cited : (218)

References (32)
  • 1
    • 0030901637 scopus 로고    scopus 로고
    • Structure of the adenylyl cyclase catalytic core
    • Zhang G, Liu Y, Ruoho AE, Hurley JH. Structure of the adenylyl cyclase catalytic core. Nature. 386:1997;247-253.
    • (1997) Nature , vol.386 , pp. 247-253
    • Zhang, G.1    Liu, Y.2    Ruoho, A.E.3    Hurley, J.H.4
  • 2
    • 0030745322 scopus 로고    scopus 로고
    • A polymerase I palm in adenylyl cyclase?
    • of special interest. This correspondence and its reply [3] present polar opinions on the significance of structural similarities and its evolutionary (mis)interpretation.
    • Artymiuk PJ, Poirrette AR, Rice DW, Willett P. A polymerase I palm in adenylyl cyclase? of special interest Nature. 388:1997;33-34 This correspondence and its reply [3] present polar opinions on the significance of structural similarities and its evolutionary (mis)interpretation.
    • (1997) Nature , vol.388 , pp. 33-34
    • Artymiuk, P.J.1    Poirrette, A.R.2    Rice, D.W.3    Willett, P.4
  • 3
    • 84984765670 scopus 로고    scopus 로고
    • A polymerase I palm in adenylyl cyclase? - Reply
    • of special interest. See annotation to [2].
    • Bryant SH, Madej T, Janin J, Liu Y, Ruoho AE, Zhang G, Hurley JH. A polymerase I palm in adenylyl cyclase? - reply. of special interest Nature. 388:1997;34 See annotation to [2].
    • (1997) Nature , vol.388 , pp. 34
    • Bryant, S.H.1    Madej, T.2    Janin, J.3    Liu, Y.4    Ruoho, A.E.5    Zhang, G.6    Hurley, J.H.7
  • 4
    • 2642689663 scopus 로고    scopus 로고
    • sα·GTPγS
    • of special interest. of outstanding interest. This paper also includes the structure determination of a nucleotide inhibitor bound to the active site of adenylyl cyclase. This can be compared with the nucleotide-loaded complexes of DNA polymerases [6,7].
    • sα·GTPγS. of outstanding interest Science. 278:1997;1907-1916 This paper also includes the structure determination of a nucleotide inhibitor bound to the active site of adenylyl cyclase. This can be compared with the nucleotide-loaded complexes of DNA polymerases [6,7].
    • (1997) Science , vol.278 , pp. 1907-1916
    • Tesmer, J.J.T.1    Sunahara, R.K.2    Gilman, A.G.3    Sprang, S.R.4
  • 5
    • 0031587827 scopus 로고    scopus 로고
    • Crystal structure of a pol α family replication DNA polymerase from bacteriophage RB69
    • of special interest. This first structure of DNA polymerase from a bacteriophage reveals its similarities to bacterial polymerases, with respect to overall domain organization, with remarkable variations in the structures of individual homologous domains.
    • Wang J, Sattar AKMA, Wang CC, Karam JD, Konigsberg WH, Steitz TA. Crystal structure of a pol α family replication DNA polymerase from bacteriophage RB69. of special interest Cell. 89:1997;1087-1099 This first structure of DNA polymerase from a bacteriophage reveals its similarities to bacterial polymerases, with respect to overall domain organization, with remarkable variations in the structures of individual homologous domains.
    • (1997) Cell , vol.89 , pp. 1087-1099
    • Wang, J.1    Sattar, A.K.M.A.2    Wang, C.C.3    Karam, J.D.4    Konigsberg, W.H.5    Steitz, T.A.6
  • 6
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution
    • of special interest. These new structures (see also [7]) provide details as to how DNA polymerases bind to and reshape their substrates.
    • Doublié S, Tabor S, Long AM, Richardson CC, Ellenberg T. Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution. of special interest Nature. 391:1997;251-258 These new structures (see also [7]) provide details as to how DNA polymerases bind to and reshape their substrates.
    • (1997) Nature , vol.391 , pp. 251-258
    • Doublié, S.1    Tabor, S.2    Long, A.M.3    Richardson, C.C.4    Ellenberg, T.5
  • 7
    • 0032518524 scopus 로고    scopus 로고
    • Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystals
    • of special interest. See annotation to [6].
    • Kiefer JR, Mao C, Braman JC, Beese LS. Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystals. of special interest Nature. 391:1997;304-307 See annotation to [6].
    • (1997) Nature , vol.391 , pp. 304-307
    • Kiefer, J.R.1    Mao, C.2    Braman, J.C.3    Beese, L.S.4
  • 8
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin AG, Brenner SE, Hubbard T, Chothia C. SCOP: a structural classification of proteins database for the investigation of sequences and structures. J Mol Biol. 247:1995;536-540.
    • (1995) J Mol Biol , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 9
    • 0030691115 scopus 로고    scopus 로고
    • The structure of ClpP at 2.3 Å resolution suggests a model for ATP-dependent proteolysis
    • of outstanding interest. The most remarkable aspect of this structure is that it shows convergent relationships with other proteases and a divergent relationship with an enzyme in the β-oxidation pathway of fatty acids.
    • Wang J, Hartling JA, Flanagan JM. The structure of ClpP at 2.3 Å resolution suggests a model for ATP-dependent proteolysis. of outstanding interest Cell. 91:1997;447-456 The most remarkable aspect of this structure is that it shows convergent relationships with other proteases and a divergent relationship with an enzyme in the β-oxidation pathway of fatty acids.
    • (1997) Cell , vol.91 , pp. 447-456
    • Wang, J.1    Hartling, J.A.2    Flanagan, J.M.3
  • 10
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution
    • Lowe J, Stock D, Jap B, Zwickl P, Baumeister W, Huber R. Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution. Science. 268:1995;533-539.
    • (1995) Science , vol.268 , pp. 533-539
    • Lowe, J.1    Stock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 12
    • 0030925223 scopus 로고    scopus 로고
    • Crystal structure of heat shock locus V (HsIV) from Escherichia coli
    • of special interest. The determination of its structure confirms that HsIV is a prokaryotic homologue of the 20S proteasome [10,11].
    • Bochtier M, Ditzel L, Groll M, Huber R. Crystal structure of heat shock locus V (HsIV) from Escherichia coli. of special interest Proc Natl Acad Sci USA. 94:1997;6070-6074 The determination of its structure confirms that HsIV is a prokaryotic homologue of the 20S proteasome [10,11].
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6070-6074
    • Bochtier, M.1    Ditzel, L.2    Groll, M.3    Huber, R.4
  • 13
    • 0029791410 scopus 로고    scopus 로고
    • The crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 Å resolution: A spiral fold defines the CoA-binding pocket
    • Engel CK, Kiema TR, Zeelen JP, Hiltunen JK, Wierenga RK. The crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 Å resolution: a spiral fold defines the CoA-binding pocket. EMBO J. 15:1996;5135-5145.
    • (1996) EMBO J , vol.15 , pp. 5135-5145
    • Engel, C.K.1    Kiema, T.R.2    Zeelen, J.P.3    Hiltunen, J.K.4    Wierenga, R.K.5
  • 14
    • 0032488815 scopus 로고    scopus 로고
    • Crystal structure of enoyl-CoA hydratase complexed with octanoyl-CoA reveals the structural adaptations required for binding of a long chain fatty acid-CoA molecule
    • of special interest. This new structure of a crotonase - inhibitor complex shows the enzyme's active site in more detail and confirms the proposed catalytic mechanism.
    • Engel CK, Mathieu M, Zeelen JP, Hiltunen JK, Wierenga RK. Crystal structure of enoyl-CoA hydratase complexed with octanoyl-CoA reveals the structural adaptations required for binding of a long chain fatty acid-CoA molecule. of special interest J Mol Biol. 275:1998;847-859 This new structure of a crotonase - inhibitor complex shows the enzyme's active site in more detail and confirms the proposed catalytic mechanism.
    • (1998) J Mol Biol , vol.275 , pp. 847-859
    • Engel, C.K.1    Mathieu, M.2    Zeelen, J.P.3    Hiltunen, J.K.4    Wierenga, R.K.5
  • 15
    • 0030037645 scopus 로고    scopus 로고
    • Structure of 4-chlorobenzoyl coenzyme A dehalogenase determined to 1.8 Å resolution: An enzyme catalyst generated via adaptive mutation
    • Benning MM, Taylor KL, Liu R-Q, Yang G, Xiang H, Wesenberg G, Dunaway-Mariano D, Holden HM. Structure of 4-chlorobenzoyl coenzyme A dehalogenase determined to 1.8 Å resolution: an enzyme catalyst generated via adaptive mutation. Biochemistry. 35:1996;8103-8109.
    • (1996) Biochemistry , vol.35 , pp. 8103-8109
    • Benning, M.M.1    Taylor, K.L.2    Liu R-Q3    Yang, G.4    Xiang, H.5    Wesenberg, G.6    Dunaway-Mariano, D.7    Holden, H.M.8
  • 17
    • 0021285466 scopus 로고
    • 5-3-ketosteroid isomerase: Architecture and location of the active centre
    • 5-3-ketosteroid isomerase: architecture and location of the active centre. J Biol Chem. 259:1984;9096-9103.
    • (1984) J Biol Chem , vol.259 , pp. 9096-9103
    • Westbrook, E.M.1    Piro, O.E.2    Sigler, P.B.3
  • 19
    • 0001305507 scopus 로고    scopus 로고
    • 5-3-ketosteroid isomerase with and without a reaction intermediate analogue
    • of outstanding interest. This long awaited structure, determined in both crystal and solution [18], has revealed the environment of a low barrier hydrogen bond within the active site.
    • 5-3-ketosteroid isomerase with and without a reaction intermediate analogue. of outstanding interest Biochemistry. 36:1997;14030-14036 This long awaited structure, determined in both crystal and solution [18], has revealed the environment of a low barrier hydrogen bond within the active site.
    • (1997) Biochemistry , vol.36 , pp. 14030-14036
    • Kim, S.W.1    Cha S-S2    Cho H-S3    Kim J-S4    Ha N-C5    Cho M-J6    Joo, S.7    Kim, K.K.8    Choi, K.Y.9    Oh B-H10
  • 20
    • 0028774336 scopus 로고
    • Crystal structure of scytalone dehydratase - A disease determinant of the rice pathogen, Magnaporthe grisea
    • Lundqvist T, Rice J, Hodge CN, Basarab GS, Pierce J, Lindqvist Y. Crystal structure of scytalone dehydratase - a disease determinant of the rice pathogen, Magnaporthe grisea. Structure. 2:1994;937-944.
    • (1994) Structure , vol.2 , pp. 937-944
    • Lundqvist, T.1    Rice, J.2    Hodge, C.N.3    Basarab, G.S.4    Pierce, J.5    Lindqvist, Y.6
  • 21
    • 0030593377 scopus 로고    scopus 로고
    • The 1.6 Å structure of nuclear transport factor 2 (NTF2)
    • Bullock TL, Clarkson WD, Kent HM, Stewart M. The 1.6 Å structure of nuclear transport factor 2 (NTF2). J Mol Biol. 260:1996;422-431.
    • (1996) J Mol Biol , vol.260 , pp. 422-431
    • Bullock, T.L.1    Clarkson, W.D.2    Kent, H.M.3    Stewart, M.4
  • 22
    • 0029950031 scopus 로고    scopus 로고
    • Structural classification of proteins: New superfamilies
    • Murzin AG. Structural classification of proteins: new superfamilies. Curr Opin Struct Biol. 6:1996;386-394.
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 386-394
    • Murzin, A.G.1
  • 24
    • 0031569353 scopus 로고    scopus 로고
    • 2, a bacterial enzyme with application in cancer therapy
    • 2 has structural homology with other zinc-dependent exopeptidases, both those that have a single zinc ion and those with a pair of zinc ions in the active site.
    • 2 has structural homology with other zinc-dependent exopeptidases, both those that have a single zinc ion and those with a pair of zinc ions in the active site.
    • (1997) Structure , vol.5 , pp. 337-347
    • Rowsell, S.1    Paupit, R.A.2    Tucker, A.D.3    Melton, R.G.4    Blow, D.M.5    Brick, P.6
  • 25
    • 0028773280 scopus 로고
    • Crystal structure of Aeromonas proteolytica aminopeptidase: A prototypical member of the co-catalytic zinc enzyme family
    • Chevrier B, Schalk C, D'Orchymont H, Rondeau J-M, Moras D, Tarnus C. Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical member of the co-catalytic zinc enzyme family. Structure. 2:1994;283-291.
    • (1994) Structure , vol.2 , pp. 283-291
    • Chevrier, B.1    Schalk, C.2    D'Orchymont, H.3    Rondeau J-M4    Moras, D.5    Tarnus, C.6
  • 26
    • 0030666566 scopus 로고    scopus 로고
    • Structure of the thrombin complex with triabin, a lipocalin-like exocite-binding inhibitor derived from a triatomine bug
    • of outstanding interest. The structure determination of triabin has provided the first example of very probably homologous proteins with distinct topologies.
    • Fuentes-Prior P, Noeske-Jungblut C, Donner P, Schleuning W-D, Huber R, Bode W. Structure of the thrombin complex with triabin, a lipocalin-like exocite-binding inhibitor derived from a triatomine bug. of outstanding interest Proc Natl Acad Sci USA. 94:1997;11845-11850 The structure determination of triabin has provided the first example of very probably homologous proteins with distinct topologies.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11845-11850
    • Fuentes-Prior, P.1    Noeske-Jungblut, C.2    Donner, P.3    Schleuning W-D4    Huber, R.5    Bode, W.6
  • 27
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • of special interest. The results of a PSI-BLAST search may complement those of structure similarity searches.
    • Altschul SA, Madden TL, Schäffer AA, Zhang J, Zhang Z, Miller W, Lipman DJ. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. of special interest Nucleic Acids Res. 25:1997;3389-3402 The results of a PSI-BLAST search may complement those of structure similarity searches.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.A.1    Madden, T.L.2    Schäffer, A.A.3    Zhang, J.4    Zhang, Z.5    Miller, W.6    Lipman, D.J.7
  • 28
    • 0028348081 scopus 로고
    • Principles determining the structure of β-sheet barrels in proteins
    • Murzin AG, Lesk AM, Chothia C. Principles determining the structure of β-sheet barrels in proteins. J Mol Biol. 236:1994;1369-1400.
    • (1994) J Mol Biol , vol.236 , pp. 1369-1400
    • Murzin, A.G.1    Lesk, A.M.2    Chothia, C.3
  • 30
    • 0031574021 scopus 로고    scopus 로고
    • Biological identity and diversity in photosynthesis and respiration: Structure of the lumen-side domain of the chloroplast Rieske protein
    • of outstanding interest. A comparison of the structures and sequences of the soluble domains of chloroplast and mitochondria Rieske proteins (see also [28]) has revealed the segregation of structural conservation and divergence in different subdomains.
    • Carrell CJ, Zhang H, Cramer WA, Smith JL. Biological identity and diversity in photosynthesis and respiration: structure of the lumen-side domain of the chloroplast Rieske protein. of outstanding interest Structure. 5:1997;1613-1625 A comparison of the structures and sequences of the soluble domains of chloroplast and mitochondria Rieske proteins (see also [28]) has revealed the segregation of structural conservation and divergence in different subdomains.
    • (1997) Structure , vol.5 , pp. 1613-1625
    • Carrell, C.J.1    Zhang, H.2    Cramer, W.A.3    Smith, J.L.4
  • 31
    • 0000977124 scopus 로고
    • Relative orientation of close-packed β-pleated sheets in proteins
    • Chothia C, Janin J. Relative orientation of close-packed β-pleated sheets in proteins. Proc Natl Acad Sci USA. 78:1981;4146-4150.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 4146-4150
    • Chothia, C.1    Janin, J.2
  • 32
    • 0032536003 scopus 로고    scopus 로고
    • Immediate release of crystallographic data: A proposal
    • of special interest. By citing this letter, the author wishes to express his support for the title proposal.
    • Wlodawer A, Davies D, Petsco G, Rossmann G, Olson A, Sussman JL. Immediate release of crystallographic data: a proposal. of special interest Science. 279:1998;306-307 By citing this letter, the author wishes to express his support for the title proposal.
    • (1998) Science , vol.279 , pp. 306-307
    • Wlodawer, A.1    Davies, D.2    Petsco, G.3    Rossmann, G.4    Olson, A.5    Sussman, J.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.