메뉴 건너뛰기




Volumn 60, Issue 4, 2005, Pages 778-786

Crystal structure of YHI9, the yeast member of the phenazine biosynthesis PhzF enzyme superfamily

Author keywords

Domain swapping; Gene duplication and fusion; PhzF family

Indexed keywords

ANTIBIOTIC AGENT; ANTIFUNGAL AGENT; DIAMINOPIMELATE EPIMERASE; DIAMINOPIMELIC ACID; EPIMERASE; FUNGAL ENZYME; PHENAZINE; PHZF PROTEIN; UNCLASSIFIED DRUG;

EID: 24644521523     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20548     Document Type: Article
Times cited : (10)

References (27)
  • 2
    • 0033534534 scopus 로고    scopus 로고
    • Molecular mechanisms of bacterial virulence elucidated using a Pseudomonas aeruginosa-Caenorhabditis elegans pathogenesis model
    • Mahajan-Miklos S, Tan MW, Rahme LG, Ausubel FM. Molecular mechanisms of bacterial virulence elucidated using a Pseudomonas aeruginosa-Caenorhabditis elegans pathogenesis model. Cell 1999;96:47-56.
    • (1999) Cell , vol.96 , pp. 47-56
    • Mahajan-Miklos, S.1    Tan, M.W.2    Rahme, L.G.3    Ausubel, F.M.4
  • 4
    • 0035685204 scopus 로고    scopus 로고
    • Functional analysis of genes for biosynthesis of pyocyanin and phenazine-1-carboxamide from Pseudomonas aeruginosa PAO1
    • Mavrodi DV, Bonsall RF, Delaney SM, Soule MJ, Phillips G, Thomashow LS. Functional analysis of genes for biosynthesis of pyocyanin and phenazine-1-carboxamide from Pseudomonas aeruginosa PAO1. J Bacteriol 2001;183:6454-6465.
    • (2001) J Bacteriol , vol.183 , pp. 6454-6465
    • Mavrodi, D.V.1    Bonsall, R.F.2    Delaney, S.M.3    Soule, M.J.4    Phillips, G.5    Thomashow, L.S.6
  • 5
    • 0035955225 scopus 로고    scopus 로고
    • Phenazine biosynthesis in Pseudomonas fluorescens: Branchpoint from the primary shikimate biosynthetic pathway and role of phenazine-1,6-dicarboxylic acid
    • McDonald M, Mavrodi DV, Thomashow LS, Floss HG. Phenazine biosynthesis in Pseudomonas fluorescens: branchpoint from the primary shikimate biosynthetic pathway and role of phenazine-1,6-dicarboxylic acid. J Am Chem Soc 2001;123:9459-9460.
    • (2001) J Am Chem Soc , vol.123 , pp. 9459-9460
    • McDonald, M.1    Mavrodi, D.V.2    Thomashow, L.S.3    Floss, H.G.4
  • 6
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure
    • Hendrickson WA, Horton JR, Lemaster DM. Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure Embo J 1990;9:1665-1672.
    • (1990) Embo J , vol.9 , pp. 1665-1672
    • Hendrickson, W.A.1    Horton, J.R.2    Lemaster, D.M.3
  • 7
    • 0003076963 scopus 로고
    • Recent changes to the MOSFLM package for processing film and image plate data Joint CCP4 + ESF-EAMCB
    • Leslie AGW. Recent changes to the MOSFLM package for processing film and image plate data Joint CCP4 + ESF-EAMCB Newsletter on Protein Crystallography 1992;26.
    • (1992) Newsletter on Protein Crystallography , pp. 26
    • Leslie, A.G.W.1
  • 8
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project N. 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
  • 10
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, 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    Kjeldgaard, M.2
  • 11
    • 2442451688 scopus 로고    scopus 로고
    • Crystal structure of E. coli yddE protein reveals a striking homology with diaminopimelate epimerase
    • Grassick A, Sulzenbacher G, Roig-Zamboni V, Campanacci V, Cambillau C, Bourne Y. Crystal structure of E. coli yddE protein reveals a striking homology with diaminopimelate epimerase. Proteins 2004;55:764-767.
    • (2004) Proteins , vol.55 , pp. 764-767
    • Grassick, A.1    Sulzenbacher, G.2    Roig-Zamboni, V.3    Campanacci, V.4    Cambillau, C.5    Bourne, Y.6
  • 12
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee B, Richards FM. The interpretation of protein structures: estimation of static accessibility. J Mol Biol 1971;55:379-400.
    • (1971) J Mol Biol , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 13
    • 0032564314 scopus 로고    scopus 로고
    • Structural symmetry, the three-dimensional structure of Haemophilus influenzae diaminopimelate epimerase
    • Cirilli M, Zheng R, Scapin G, Blanchard JS. Structural symmetry, the three-dimensional structure of Haemophilus influenzae diaminopimelate epimerase. Biochemistry 1998;37:16452-16458.
    • (1998) Biochemistry , vol.37 , pp. 16452-16458
    • Cirilli, M.1    Zheng, R.2    Scapin, G.3    Blanchard, J.S.4
  • 14
    • 0034725413 scopus 로고    scopus 로고
    • Identification of active site cysteine residues that function as general bases: Diaminopimelate epimerase
    • Koo CW, Sutherland A, Vederas JC, Blanchard JS. Identification of active site cysteine residues that function as general bases: Diaminopimelate epimerase. J Am Chem Soc 2000;122:6122-6123.
    • (2000) J Am Chem Soc , vol.122 , pp. 6122-6123
    • Koo, C.W.1    Sutherland, A.2    Vederas, J.C.3    Blanchard, J.S.4
  • 15
    • 4644249050 scopus 로고    scopus 로고
    • Refinement of Haemophilus influenzae diaminopimelic acid epimerase (DapF) at 1.75 Å resolution suggests a mechanism for stereocontrol during catalysis
    • Lloyd AJ, Huyton T, Turkenburg J, Roper DI. Refinement of Haemophilus influenzae diaminopimelic acid epimerase (DapF) at 1.75 Å resolution suggests a mechanism for stereocontrol during catalysis. Acta Crystallogr D Biol Crystallogr 2004;60:397-400.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 397-400
    • Lloyd, A.J.1    Huyton, T.2    Turkenburg, J.3    Roper, D.I.4
  • 16
    • 4344560669 scopus 로고    scopus 로고
    • The purification, crystallization and preliminary structural characterization of PhzF, a key enzyme in the phenazine-biosynthesis pathway from Pseudomonas fluorescens 2-79
    • Mavrodi DV, Bleimling N, Thomashow LS, Blankenfeldt W. The purification, crystallization and preliminary structural characterization of PhzF, a key enzyme in the phenazine-biosynthesis pathway from Pseudomonas fluorescens 2-79. Acta Crystallogr D Biol Crystallogr 2004;60:184-186.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 184-186
    • Mavrodi, D.V.1    Bleimling, N.2    Thomashow, L.S.3    Blankenfeldt, W.4
  • 17
    • 0036301494 scopus 로고    scopus 로고
    • Crystal structure of aspartate racemase from Pyrococcus horikoshii OT3 and its implications for molecular mechanism of PLP-independent racemization
    • Liu L, Iwata K, Kita A, Kawarabayasi Y, Yohda M, Miki K. Crystal structure of aspartate racemase from Pyrococcus horikoshii OT3 and its implications for molecular mechanism of PLP-independent racemization. J Mol Biol 2002;319:479-489.
    • (2002) J Mol Biol , vol.319 , pp. 479-489
    • Liu, L.1    Iwata, K.2    Kita, A.3    Kawarabayasi, Y.4    Yohda, M.5    Miki, K.6
  • 18
    • 0037174167 scopus 로고    scopus 로고
    • Structural insight into gene duplication, gene fusion and domain swapping in the evolution of PLP-independent amino acid racemases
    • Liu L, Iwata K, Yohda M, Miki K. Structural insight into gene duplication, gene fusion and domain swapping in the evolution of PLP-independent amino acid racemases. FEBS Lett 2002;528:114-118.
    • (2002) FEBS Lett , vol.528 , pp. 114-118
    • Liu, L.1    Iwata, K.2    Yohda, M.3    Miki, K.4
  • 19
    • 0242290213 scopus 로고    scopus 로고
    • The structure of 4-hydroxybenzoyl-CoA thioesterase from arthrobacter sp. strain SU
    • Thoden JB, Zhuang Z, Dunaway-Mariano D, Holden HM. The structure of 4-hydroxybenzoyl-CoA thioesterase from arthrobacter sp. strain SU. J Biol Chem 2003;278:43709-43716.
    • (2003) J Biol Chem , vol.278 , pp. 43709-43716
    • Thoden, J.B.1    Zhuang, Z.2    Dunaway-Mariano, D.3    Holden, H.M.4
  • 20
    • 0030584655 scopus 로고    scopus 로고
    • Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: Two catalytic activities in one active site
    • Leesong M, Henderson BS, Gillig JR, Schwab JM, Smith JL. Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site. Structure 1996;4:253-264.
    • (1996) Structure , vol.4 , pp. 253-264
    • Leesong, M.1    Henderson, B.S.2    Gillig, J.R.3    Schwab, J.M.4    Smith, J.L.5
  • 21
    • 0033936807 scopus 로고    scopus 로고
    • Crystal structure of the Escherichia coli thioesterase II, a homolog of the human Nef binding enzyme
    • Li J, Derewenda U, Dauter Z, Smith S, Derewenda ZS. Crystal structure of the Escherichia coli thioesterase II, a homolog of the human Nef binding enzyme. Nat Struct Biol 2000;7:555-559.
    • (2000) Nat Struct Biol , vol.7 , pp. 555-559
    • Li, J.1    Derewenda, U.2    Dauter, Z.3    Smith, S.4    Derewenda, Z.S.5
  • 23
    • 0036606138 scopus 로고    scopus 로고
    • Dominant genetic screen for cofactors that enhance antisense RNA-mediated gene silencing in fission yeast
    • Raponi M, Arndt GM. Dominant genetic screen for cofactors that enhance antisense RNA-mediated gene silencing in fission yeast. Nucleic Acids Res 2002;30:2546-2554.
    • (2002) Nucleic Acids Res , vol.30 , pp. 2546-2554
    • Raponi, M.1    Arndt, G.M.2
  • 24
    • 4744365340 scopus 로고    scopus 로고
    • Structure and function of the phenazine biosynthesis protein PhzF from Pseudomonas fluorescens 2-79
    • Parsons JF, Song F, Parsons L, Calabrese K, Eisenstein E, Ladner JE. Structure and function of the phenazine biosynthesis protein PhzF from Pseudomonas fluorescens 2-79. Biochemistry 2004;43:12427-12435.
    • (2004) Biochemistry , vol.43 , pp. 12427-12435
    • Parsons, J.F.1    Song, F.2    Parsons, L.3    Calabrese, K.4    Eisenstein, E.5    Ladner, J.E.6
  • 26
    • 0028181017 scopus 로고
    • An algorithm for automatically generating protein topology cartoons
    • Flores TP, Moss DS, Thornton JM. An algorithm for automatically generating protein topology cartoons. Protein Eng 1994;7:31-37.
    • (1994) Protein Eng , vol.7 , pp. 31-37
    • Flores, T.P.1    Moss, D.S.2    Thornton, J.M.3
  • 27
    • 2542445427 scopus 로고    scopus 로고
    • ConSurf: Identification of functional regions in proteins by surface-mapping of phylogenetic information
    • Glaser F, Pupko T, Paz I, Bell RE, Bechor-Shental D, Martz E, Ben-Tal N. ConSurf: identification of functional regions in proteins by surface-mapping of phylogenetic information. Bioinformatics 2003;19:163-164.
    • (2003) Bioinformatics , vol.19 , pp. 163-164
    • Glaser, F.1    Pupko, T.2    Paz, I.3    Bell, R.E.4    Bechor-Shental, D.5    Martz, E.6    Ben-Tal, N.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.