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Volumn 112, Issue 6, 2015, Pages E576-E585

Structure and mechanism of staphylococcus aureus TarM, the wall teichoic acid α-glycosyltransferase

Author keywords

Bacterial pathogenicity; Cell wall; Crystal structure; Glycosyltransferase; Wall teichoic acid

Indexed keywords

GLYCOSYLTRANSFERASE; TEICHOIC ACID; BACTERIAL PROTEIN; METAL;

EID: 84922606932     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1418084112     Document Type: Article
Times cited : (49)

References (67)
  • 1
    • 0347479228 scopus 로고    scopus 로고
    • A continuum of anionic charge: Structures and functions of D-alanyl-teichoic acids in gram-positive bacteria
    • Neuhaus FC, Baddiley J (2003) A continuum of anionic charge: Structures and functions of D-alanyl-teichoic acids in gram-positive bacteria. Microbiol Mol Biol Rev 67(4):686-723.
    • (2003) Microbiol Mol Biol Rev , vol.67 , Issue.4 , pp. 686-723
    • Neuhaus, F.C.1    Baddiley, J.2
  • 2
    • 40949089662 scopus 로고    scopus 로고
    • Teichoic acids and related cell-wall glycopolymers in Gram-positive physiology and host interactions
    • Weidenmaier C, Peschel A (2008) Teichoic acids and related cell-wall glycopolymers in Gram-positive physiology and host interactions. Nat Rev Microbiol 6(4):276-287.
    • (2008) Nat Rev Microbiol , vol.6 , Issue.4 , pp. 276-287
    • Weidenmaier, C.1    Peschel, A.2
  • 3
    • 0021939769 scopus 로고
    • Structure of the linkage units between ribitol teichoic acids and peptidoglycan
    • Kojima N, Araki Y, Ito E (1985) Structure of the linkage units between ribitol teichoic acids and peptidoglycan. J Bacteriol 161(1):299-306.
    • (1985) J Bacteriol , vol.161 , Issue.1 , pp. 299-306
    • Kojima, N.1    Araki, Y.2    Ito, E.3
  • 5
    • 2342639647 scopus 로고    scopus 로고
    • Role of teichoic acids in Staphylococcus aureus nasal colonization, a major risk factor in nosocomial infections
    • Weidenmaier C, et al. (2004) Role of teichoic acids in Staphylococcus aureus nasal colonization, a major risk factor in nosocomial infections. Nat Med 10(3):243-245.
    • (2004) Nat Med , vol.10 , Issue.3 , pp. 243-245
    • Weidenmaier, C.1
  • 6
    • 18544385333 scopus 로고    scopus 로고
    • Lack of wall teichoic acids in Staphylococcus aureus leads to reduced interactions with endothelial cells and to attenuated virulence in a rabbit model of endocarditis
    • Weidenmaier C, et al. (2005) Lack of wall teichoic acids in Staphylococcus aureus leads to reduced interactions with endothelial cells and to attenuated virulence in a rabbit model of endocarditis. J Infect Dis 191(10):1771-1777.
    • (2005) J Infect Dis , vol.191 , Issue.10 , pp. 1771-1777
    • Weidenmaier, C.1
  • 7
    • 58149479227 scopus 로고    scopus 로고
    • Pleiotropic roles of polyglycerolphosphate synthase of lipoteichoic acid in growth of Staphylococcus aureus cells
    • Oku Y, et al. (2009) Pleiotropic roles of polyglycerolphosphate synthase of lipoteichoic acid in growth of Staphylococcus aureus cells. J Bacteriol 191(1):141-151.
    • (2009) J Bacteriol , vol.191 , Issue.1 , pp. 141-151
    • Oku, Y.1
  • 8
    • 0033806585 scopus 로고    scopus 로고
    • The D-alanine residues of Staphylococcus aureus teichoic acids alter the susceptibility to vancomycin and the activity of autolytic enzymes
    • Peschel A, Vuong C, Otto M, Götz F (2000) The D-alanine residues of Staphylococcus aureus teichoic acids alter the susceptibility to vancomycin and the activity of autolytic enzymes. Antimicrob Agents Chemother 44(10):2845-2847.
    • (2000) Antimicrob Agents Chemother , vol.44 , Issue.10 , pp. 2845-2847
    • Peschel, A.1    Vuong, C.2    Otto, M.3    Götz, F.4
  • 9
    • 67649413346 scopus 로고    scopus 로고
    • Wall teichoic acid protects Staphylococcus aureus against antimicrobial fatty acids from human skin
    • Kohler T, Weidenmaier C, Peschel A (2009) Wall teichoic acid protects Staphylococcus aureus against antimicrobial fatty acids from human skin. J Bacteriol 191(13):4482-4484.
    • (2009) J Bacteriol , vol.191 , Issue.13 , pp. 4482-4484
    • Kohler, T.1    Weidenmaier, C.2    Peschel, A.3
  • 10
    • 0033605557 scopus 로고    scopus 로고
    • Inactivation of the dlt operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides
    • Peschel A, et al. (1999) Inactivation of the dlt operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides. J Biol Chem 274(13):8405-8410.
    • (1999) J Biol Chem , vol.274 , Issue.13 , pp. 8405-8410
    • Peschel, A.1
  • 11
    • 33845941753 scopus 로고    scopus 로고
    • Influence of wall teichoic acid on lysozyme resistance in Staphylococcus aureus
    • Bera A, et al. (2007) Influence of wall teichoic acid on lysozyme resistance in Staphylococcus aureus. J Bacteriol 189(1):280-283.
    • (2007) J Bacteriol , vol.189 , Issue.1 , pp. 280-283
    • Bera, A.1
  • 12
    • 0017519550 scopus 로고
    • Function of cell wall teichoic acid in thermally injured Staphylococcus aureus
    • Hoover DG, Gray RJ (1977) Function of cell wall teichoic acid in thermally injured Staphylococcus aureus. J Bacteriol 131(2):477-485.
    • (1977) J Bacteriol , vol.131 , Issue.2 , pp. 477-485
    • Hoover, D.G.1    Gray, R.J.2
  • 13
    • 0018906115 scopus 로고
    • Role of teichoic acid in the binding of Staphylococcus aureus to nasal epithelial cells
    • Aly R, Shinefield HR, Litz C, Maibach HI (1980) Role of teichoic acid in the binding of Staphylococcus aureus to nasal epithelial cells. J Infect Dis 141(4):463-465.
    • (1980) J Infect Dis , vol.141 , Issue.4 , pp. 463-465
    • Aly, R.1    Shinefield, H.R.2    Litz, C.3    Maibach, H.I.4
  • 14
    • 0035808774 scopus 로고    scopus 로고
    • Structure-function relationship of cytokine induction by lipoteichoic acid from Staphylococcus aureus
    • Morath S, Geyer A, Hartung T (2001) Structure-function relationship of cytokine induction by lipoteichoic acid from Staphylococcus aureus. J Exp Med 193(3):393-397.
    • (2001) J Exp Med , vol.193 , Issue.3 , pp. 393-397
    • Morath, S.1    Geyer, A.2    Hartung, T.3
  • 15
    • 13444280215 scopus 로고    scopus 로고
    • CD36 is a sensor of diacylglycerides
    • Hoebe K, et al. (2005) CD36 is a sensor of diacylglycerides. Nature 433(7025):523-527.
    • (2005) Nature , vol.433 , Issue.7025 , pp. 523-527
    • Hoebe, K.1
  • 16
    • 41649107808 scopus 로고    scopus 로고
    • Cytokine induction by Gram-positive bacteria
    • Draing C, et al. (2008) Cytokine induction by Gram-positive bacteria. Immunobiology 213(3-4):285-296.
    • (2008) Immunobiology , vol.213 , Issue.3-4 , pp. 285-296
    • Draing, C.1
  • 17
    • 0014519589 scopus 로고
    • Use of bacteriophage-resistant mutants to study the nature of the bacteriophage receptor site of Staphylococcus aureus
    • Chatterjee AN (1969) Use of bacteriophage-resistant mutants to study the nature of the bacteriophage receptor site of Staphylococcus aureus. J Bacteriol 98(2):519-527.
    • (1969) J Bacteriol , vol.98 , Issue.2 , pp. 519-527
    • Chatterjee, A.N.1
  • 19
    • 0035059332 scopus 로고    scopus 로고
    • Key role of teichoic acid net charge in Staphylococcus aureus colonization of artificial surfaces
    • Gross M, Cramton SE, Götz F, Peschel A (2001) Key role of teichoic acid net charge in Staphylococcus aureus colonization of artificial surfaces. Infect Immun 69(5):3423-3426.
    • (2001) Infect Immun , vol.69 , Issue.5 , pp. 3423-3426
    • Gross, M.1    Cramton, S.E.2    Götz, F.3    Peschel, A.4
  • 20
    • 0005112472 scopus 로고
    • Teichoic acids in walls and cells of grampositive bacteria
    • Baddiley J (1962) Teichoic acids in walls and cells of grampositive bacteria. Fed Proc 21:1084-1088.
    • (1962) Fed Proc , vol.21 , pp. 1084-1088
    • Baddiley, J.1
  • 21
    • 0345438921 scopus 로고
    • Chemical structure of teichoic acid from Staphylococcus aureus, strain Copenhagen
    • Sanderson AR, Strominger JL, Nathenson SG (1962) Chemical structure of teichoic acid from Staphylococcus aureus, strain Copenhagen. J Biol Chem 237:3603-3613.
    • (1962) J Biol Chem , vol.237 , pp. 3603-3613
    • Sanderson, A.R.1    Strominger, J.L.2    Nathenson, S.G.3
  • 22
    • 75949132759 scopus 로고
    • Separation of teichoic acid of Staphylococcus aureus into two immunologically distinct specific polysaccharides with alpha- and beta-n-acetylglucosaminyl linkages respectively. Antigenicity of theichoic acids in man
    • Torii M, Kabat EA, Bezer AE (1964) Separation of teichoic acid of Staphylococcus aureus into two immunologically distinct specific polysaccharides with alpha- and beta-n-acetylglucosaminyl linkages respectively. Antigenicity of theichoic acids in man. J Exp Med 120:13-29.
    • (1964) J Exp Med , vol.120 , pp. 13-29
    • Torii, M.1    Kabat, E.A.2    Bezer, A.E.3
  • 23
    • 73849155833 scopus 로고
    • Enzymatic synthesis and immunochemistry of N-acetylglucosaminylribitol linkages in the teichoic acids of Staphylococcus aureus stains
    • Nathenson SG, Strominger JL (1962) Enzymatic synthesis and immunochemistry of N-acetylglucosaminylribitol linkages in the teichoic acids of Staphylococcus aureus stains. J Biol Chem 237:3839-3841.
    • (1962) J Biol Chem , vol.237 , pp. 3839-3841
    • Nathenson, S.G.1    Strominger, J.L.2
  • 24
    • 0014010218 scopus 로고
    • Enzymatic synthesis and immunochemistry of alpha- and beta-N-acetylglucosaminylribitol linkages in teichoic acids from several strains of Staphylococcus aureus
    • Nathenson SG, Ishimoto N, Anderson JS, Strominger JL (1966) Enzymatic synthesis and immunochemistry of alpha- and beta-N-acetylglucosaminylribitol linkages in teichoic acids from several strains of Staphylococcus aureus. J Biol Chem 241(3):651-658.
    • (1966) J Biol Chem , vol.241 , Issue.3 , pp. 651-658
    • Nathenson, S.G.1    Ishimoto, N.2    Anderson, J.S.3    Strominger, J.L.4
  • 25
    • 77951581144 scopus 로고    scopus 로고
    • Glycosylation of wall teichoic acid in Staphylococcus aureus by TarM
    • Xia G, et al. (2010) Glycosylation of wall teichoic acid in Staphylococcus aureus by TarM. J Biol Chem 285(18):13405-13415.
    • (2010) J Biol Chem , vol.285 , Issue.18 , pp. 13405-13415
    • Xia, G.1
  • 27
    • 84869214183 scopus 로고    scopus 로고
    • Methicillin resistance in Staphylococcus aureus requires glycosylated wall teichoic acids
    • Brown S, et al. (2012) Methicillin resistance in Staphylococcus aureus requires glycosylated wall teichoic acids. Proc Natl Acad Sci USA 109(46):18909-18914.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.46 , pp. 18909-18914
    • Brown, S.1
  • 28
    • 84886715761 scopus 로고    scopus 로고
    • Glycoepitopes of staphylococcal wall teichoic acid govern complement-mediated opsonophagocytosis via human serum antibody and man-nose-binding lectin
    • Kurokawa K, et al. (2013) Glycoepitopes of staphylococcal wall teichoic acid govern complement-mediated opsonophagocytosis via human serum antibody and man-nose-binding lectin. J Biol Chem 288(43):30956-30968.
    • (2013) J Biol Chem , vol.288 , Issue.43 , pp. 30956-30968
    • Kurokawa, K.1
  • 30
    • 66249128912 scopus 로고    scopus 로고
    • A method for the analysis of domain movements in large biomolecular complexes
    • Poornam GP, Matsumoto A, Ishida H, Hayward S (2009) A method for the analysis of domain movements in large biomolecular complexes. Proteins 76(1):201-212.
    • (2009) Proteins , vol.76 , Issue.1 , pp. 201-212
    • Poornam, G.P.1    Matsumoto, A.2    Ishida, H.3    Hayward, S.4
  • 32
    • 78650950110 scopus 로고    scopus 로고
    • Processivity of cellobiohydrolases is limited by the substrate
    • Kurasin M, Väljamäe P (2011) Processivity of cellobiohydrolases is limited by the substrate. J Biol Chem 286(1):169-177.
    • (2011) J Biol Chem , vol.286 , Issue.1 , pp. 169-177
    • Kurasin, M.1    Väljamäe, P.2
  • 33
    • 33750470057 scopus 로고    scopus 로고
    • Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination
    • Vedadi M, et al. (2006) Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination. Proc Natl Acad Sci USA 103(43):15835-15840.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.43 , pp. 15835-15840
    • Vedadi, M.1
  • 34
    • 33750974777 scopus 로고    scopus 로고
    • Insights into the synthesis of lipopolysaccharide and antibiotics through the structures of two retaining glycosyltransferases from family GT4
    • Martinez-Fleites C, et al. (2006) Insights into the synthesis of lipopolysaccharide and antibiotics through the structures of two retaining glycosyltransferases from family GT4. Chem Biol 13(11):1143-1152.
    • (2006) Chem Biol , vol.13 , Issue.11 , pp. 1143-1152
    • Martinez-Fleites, C.1
  • 35
    • 0036384359 scopus 로고    scopus 로고
    • Enzymatic catalysis in crystals of Escherichia coli maltodextrin phosphorylase
    • Geremia S, Campagnolo M, Schinzel R, Johnson LN (2002) Enzymatic catalysis in crystals of Escherichia coli maltodextrin phosphorylase. J Mol Biol 322(2):413-423.
    • (2002) J Mol Biol , vol.322 , Issue.2 , pp. 413-423
    • Geremia, S.1    Campagnolo, M.2    Schinzel, R.3    Johnson, L.N.4
  • 36
    • 23944471080 scopus 로고    scopus 로고
    • Structural evidence of a passive base-flipping mechanism for AGT, an unusual GT-B glycosyltransferase
    • Larivière L, Sommer N, Moréra S (2005) Structural evidence of a passive base-flipping mechanism for AGT, an unusual GT-B glycosyltransferase. J Mol Biol 352(1):139-150.
    • (2005) J Mol Biol , vol.352 , Issue.1 , pp. 139-150
    • Larivière, L.1    Sommer, N.2    Moréra, S.3
  • 37
    • 47049105152 scopus 로고    scopus 로고
    • Structural and enzymatic analysis of MshA from Corynebacterium glutamicum: Substrate-assisted catalysis
    • Vetting MW, Frantom PA, Blanchard JS (2008) Structural and enzymatic analysis of MshA from Corynebacterium glutamicum: Substrate-assisted catalysis. J Biol Chem 283(23):15834-15844.
    • (2008) J Biol Chem , vol.283 , Issue.23 , pp. 15834-15844
    • Vetting, M.W.1    Frantom, P.A.2    Blanchard, J.S.3
  • 38
    • 76349106696 scopus 로고    scopus 로고
    • Mechanistic insight into enzymatic glycosyl transfer with retention of configuration through analysis of glycomimetic inhibitors
    • Errey JC, et al. (2010) Mechanistic insight into enzymatic glycosyl transfer with retention of configuration through analysis of glycomimetic inhibitors. Angew Chem Int Ed Engl 49(7):1234-1237.
    • (2010) Angew Chem Int Ed Engl , vol.49 , Issue.7 , pp. 1234-1237
    • Errey, J.C.1
  • 39
    • 0001403866 scopus 로고
    • Solvolysis of D-glucopyranosyl derivatives in mixtures of ethanol and 2,2,2-trifluoroethanol
    • Sinnott ML, Jencks WP (1980) Solvolysis of D-glucopyranosyl derivatives in mixtures of ethanol and 2,2,2-trifluoroethanol. J Am Chem Soc 102(6):2026-2032.
    • (1980) J Am Chem Soc , vol.102 , Issue.6 , pp. 2026-2032
    • Sinnott, M.L.1    Jencks, W.P.2
  • 40
    • 84860389788 scopus 로고    scopus 로고
    • Mechanistic evidence for a front-side, SNi-type reaction in a retaining glycosyltransferase
    • Lee SS, et al. (2011) Mechanistic evidence for a front-side, SNi-type reaction in a retaining glycosyltransferase. Nat Chem Biol 7(9):631-638.
    • (2011) Nat Chem Biol , vol.7 , Issue.9 , pp. 631-638
    • Lee, S.S.1
  • 41
    • 80855133537 scopus 로고    scopus 로고
    • The molecular mechanism of enzymatic glycosyl transfer with retention of configuration: Evidence for a short-lived oxocarbenium-like species
    • Ardèvol A, Rovira C (2011) The molecular mechanism of enzymatic glycosyl transfer with retention of configuration: Evidence for a short-lived oxocarbenium-like species. Angew Chem Int Ed Engl 50(46):10897-10901.
    • (2011) Angew Chem Int Ed Engl , vol.50 , Issue.46 , pp. 10897-10901
    • Ardèvol, A.1    Rovira, C.2
  • 42
    • 58849161857 scopus 로고    scopus 로고
    • Structure validation in chemical crystallography
    • Spek AL (2009) Structure validation in chemical crystallography. Acta Crystallogr D Biol Crystallogr 65(pt 2):148-155.
    • (2009) Acta Crystallogr D Biol Crystallogr , vol.65 , Issue.2 , pp. 148-155
    • Spek, A.L.1
  • 43
    • 50549164599 scopus 로고
    • Serological cross-reactivity between polysaccharide A and teichoic acid of Staphylococcus aureus
    • Haukenes G, Ellwood DC, Baddiley J, Oeding P (1961) Serological cross-reactivity between polysaccharide A and teichoic acid of Staphylococcus aureus. Biochim Biophys Acta 53:425-426.
    • (1961) Biochim Biophys Acta , vol.53 , pp. 425-426
    • Haukenes, G.1    Ellwood, D.C.2    Baddiley, J.3    Oeding, P.4
  • 44
    • 84891782659 scopus 로고    scopus 로고
    • Pfam: The protein families database
    • Finn RD, et al. (2014) Pfam: The protein families database. Nucleic Acids Res 42(database issue):D222-D230.
    • (2014) Nucleic Acids Res , vol.42 , Issue.DATABASE ISSUE , pp. D222-D230
    • Finn, R.D.1
  • 45
    • 84905408669 scopus 로고    scopus 로고
    • Structure of a novel O-linked N-acetyl-D-glucosamine (OGlcNAc) transferase, GtfA, reveals insights into the glycosylation of pneumococcal serine-rich repeat adhesins
    • Shi WW, et al. (2014) Structure of a novel O-linked N-acetyl-D-glucosamine (OGlcNAc) transferase, GtfA, reveals insights into the glycosylation of pneumococcal serine-rich repeat adhesins. J Biol Chem 289(30):20898-20907.
    • (2014) J Biol Chem , vol.289 , Issue.30 , pp. 20898-20907
    • Shi, W.W.1
  • 46
    • 84863566088 scopus 로고    scopus 로고
    • A role for glycosylated serine-rich repeat proteins in gram-positive bacterial pathogenesis
    • Lizcano A, Sanchez CJ, Orihuela CJ (2012) A role for glycosylated serine-rich repeat proteins in gram-positive bacterial pathogenesis. Mol Oral Microbiol 27(4):257-269.
    • (2012) Mol Oral Microbiol , vol.27 , Issue.4 , pp. 257-269
    • Lizcano, A.1    Sanchez, C.J.2    Orihuela, C.J.3
  • 47
    • 84862514333 scopus 로고    scopus 로고
    • Dual roles of FmtA in Staphylococcus aureus cell wall biosynthesis and autolysis
    • Qamar A, Golemi-Kotra D (2012) Dual roles of FmtA in Staphylococcus aureus cell wall biosynthesis and autolysis. Antimicrob Agents Chemother 56(7):3797-3805.
    • (2012) Antimicrob Agents Chemother , vol.56 , Issue.7 , pp. 3797-3805
    • Qamar, A.1    Golemi-Kotra, D.2
  • 48
    • 79960416809 scopus 로고    scopus 로고
    • Wall teichoic Acid-dependent adsorption of staphylococcal siphovirus and myovirus
    • Xia G, et al. (2011) Wall teichoic Acid-dependent adsorption of staphylococcal siphovirus and myovirus. J Bacteriol 193(15):4006-4009.
    • (2011) J Bacteriol , vol.193 , Issue.15 , pp. 4006-4009
    • Xia, G.1
  • 49
    • 84878321621 scopus 로고    scopus 로고
    • Phage cocktails and the future of phage therapy
    • Chan BK, Abedon ST, Loc-Carrillo C (2013) Phage cocktails and the future of phage therapy. Future Microbiol 8(6):769-783.
    • (2013) Future Microbiol , vol.8 , Issue.6 , pp. 769-783
    • Chan, B.K.1    Abedon, S.T.2    Loc-Carrillo, C.3
  • 50
    • 84883162392 scopus 로고    scopus 로고
    • Wall teichoic acid structure governs horizontal gene transfer between major bacterial pathogens
    • Winstel V, et al. (2013) Wall teichoic acid structure governs horizontal gene transfer between major bacterial pathogens. Nat Commun 4:2345.
    • (2013) Nat Commun , vol.4 , pp. 2345
    • Winstel, V.1
  • 51
    • 0026490256 scopus 로고
    • Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein
    • Leahy DJ, Hendrickson WA, Aukhil I, Erickson HP (1992) Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein. Science 258(5084):987-991.
    • (1992) Science , vol.258 , Issue.5084 , pp. 987-991
    • Leahy, D.J.1    Hendrickson, W.A.2    Aukhil, I.3    Erickson, H.P.4
  • 52
    • 41949119965 scopus 로고    scopus 로고
    • Late-stage polyribitol phosphate wall teichoic acid biosynthesis in Staphylococcus aureus
    • Meredith TC, Swoboda JG, Walker S (2008) Late-stage polyribitol phosphate wall teichoic acid biosynthesis in Staphylococcus aureus. J Bacteriol 190(8):3046-3056.
    • (2008) J Bacteriol , vol.190 , Issue.8 , pp. 3046-3056
    • Meredith, T.C.1    Swoboda, J.G.2    Walker, S.3
  • 53
    • 0021320747 scopus 로고
    • Determination of cell wall teichoic acid structure of staphylococci by rapid chemical and serological screening methods
    • Endl J, Seidl PH, Fiedler F, Schleifer KH (1984) Determination of cell wall teichoic acid structure of staphylococci by rapid chemical and serological screening methods. Arch Microbiol 137(3):272-280.
    • (1984) Arch Microbiol , vol.137 , Issue.3 , pp. 272-280
    • Endl, J.1    Seidl, P.H.2    Fiedler, F.3    Schleifer, K.H.4
  • 58
    • 77950793231 scopus 로고    scopus 로고
    • Experimental phasing with SHELXC/D/E: Combining chain tracing with density modification
    • Sheldrick GM (2010) Experimental phasing with SHELXC/D/E: Combining chain tracing with density modification. Acta Crystallogr D Biol Crystallogr 66(pt 4):479-485.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , Issue.4 , pp. 479-485
    • Sheldrick, G.M.1
  • 59
    • 33748337934 scopus 로고    scopus 로고
    • The Buccaneer software for automated model building. 1. Tracing protein chains
    • Cowtan K (2006) The Buccaneer software for automated model building. 1. Tracing protein chains. Acta Crystallogr D Biol Crystallogr 62(pt 9):1002-1011.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , Issue.9 , pp. 1002-1011
    • Cowtan, K.1
  • 60
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 53(pt 3): 240-255.
    • (1997) Acta Crystallogr D Biol Crystallogr , vol.53 , Issue.3 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 61
    • 0030757720 scopus 로고    scopus 로고
    • TNT refinement package
    • Tronrud DE (1997) TNT refinement package. Methods Enzymol 277:306-319.
    • (1997) Methods Enzymol , vol.277 , pp. 306-319
    • Tronrud, D.E.1
  • 62
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams PD, et al. (2010) PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66(pt 2):213-221.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , Issue.2 , pp. 213-221
    • Adams, P.D.1
  • 64
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy AJ, et al. (2007) Phaser crystallographic software. J Appl Cryst 40(pt 4):658-674.
    • (2007) J Appl Cryst , vol.40 , Issue.4 , pp. 658-674
    • McCoy, A.J.1
  • 65
    • 79953737180 scopus 로고    scopus 로고
    • Overview of the CCP4 suite and current developments
    • Winn MD, et al. (2011) Overview of the CCP4 suite and current developments. Acta Crystallogr D Biol Crystallogr 67(pt 4):235-242.
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , Issue.4 , pp. 235-242
    • Winn, M.D.1
  • 66
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • Chen VB, et al. (2010) MolProbity: All-atom structure validation for macromolecular crystallography. Acta Crystallogr D Biol Crystallogr 66(pt 1):12-21.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , Issue.1 , pp. 12-21
    • Chen, V.B.1
  • 67
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
    • Trott O, Olson AJ (2010) AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J Comput Chem 31(2):455-461.
    • (2010) J Comput Chem , vol.31 , Issue.2 , pp. 455-461
    • Trott, O.1    Olson, A.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.