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Volumn 4, Issue 3, 2009, Pages

Structure of the Archaeal Pab87 Peptidase Reveals a Novel Self-Compartmentalizing Protease Family

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDE; PEPTIDE HYDROLASE;

EID: 65549153602     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0004712     Document Type: Article
Times cited : (21)

References (46)
  • 1
    • 0036909399 scopus 로고    scopus 로고
    • Novel proteases: common themes and surprising features
    • Vandeputte-Rutten L, Gros P, (2002) Novel proteases: common themes and surprising features. Curr Opin Struct Biol 12: 704-708.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 704-708
    • Vandeputte-Rutten, L.1    Gros, P.2
  • 3
    • 35848944306 scopus 로고    scopus 로고
    • Species' of peptidases
    • Barrett AJ, Rawlings ND, (2007) 'Species' of peptidases. Biol Chem 388: 1151-1157.
    • (2007) Biol Chem , vol.388 , pp. 1151-1157
    • Barrett, A.J.1    Rawlings, N.D.2
  • 5
    • 0030614496 scopus 로고    scopus 로고
    • The ATP-dependent HslVU protease from Escherichia coli is a four-ring structure resembling the proteasome
    • Rohrwild M, Pfeifer G, Santarius U, Muller SA, Huang HC, et al.(1997) The ATP-dependent HslVU protease from Escherichia coli is a four-ring structure resembling the proteasome. Nat Struct Biol 4: 133-139.
    • (1997) Nat Struct Biol , vol.4 , pp. 133-139
    • Rohrwild, M.1    Pfeifer, G.2    Santarius, U.3    Muller, S.A.4    Huang, H.C.5
  • 6
    • 0033083967 scopus 로고    scopus 로고
    • Proteasomes and other self-compartmentalizing proteases in prokaryotes
    • De Mot R, Nagy I, Walz J, Baumeister W, (1999) Proteasomes and other self-compartmentalizing proteases in prokaryotes. Trends Microbiol 7: 88-92.
    • (1999) Trends Microbiol , vol.7 , pp. 88-92
    • De Mot, R.1    Nagy, I.2    Walz, J.3    Baumeister, W.4
  • 7
    • 0031713098 scopus 로고    scopus 로고
    • The isolated proteolytic domain of Escherichia coli ATP-dependent protease Lon exhibits the peptidase activity
    • Rasulova FS, Dergousova NI, Starkova NN, Melnikov EE, Rumsh LD, et al.(1998) The isolated proteolytic domain of Escherichia coli ATP-dependent protease Lon exhibits the peptidase activity. FEBS Lett 432: 179-181.
    • (1998) FEBS Lett , vol.432 , pp. 179-181
    • Rasulova, F.S.1    Dergousova, N.I.2    Starkova, N.N.3    Melnikov, E.E.4    Rumsh, L.D.5
  • 8
    • 0033615066 scopus 로고    scopus 로고
    • Giant proteases: beyond the proteasome
    • Yao T, Cohen RE, (1999) Giant proteases: beyond the proteasome. Curr Biol 9: R551-553.
    • (1999) Curr Biol , vol.9
    • Yao, T.1    Cohen, R.E.2
  • 9
    • 0035936157 scopus 로고    scopus 로고
    • Crystal structure of the tricorn protease reveals a protein disassembly line
    • Brandstetter H, Kim JS, Groll M, Huber R, (2001) Crystal structure of the tricorn protease reveals a protein disassembly line. Nature 414: 466-470.
    • (2001) Nature , vol.414 , pp. 466-470
    • Brandstetter, H.1    Kim, J.S.2    Groll, M.3    Huber, R.4
  • 10
    • 0033396636 scopus 로고    scopus 로고
    • Capsids of tricorn protease studied by electron cryomicroscopy
    • Walz J, Koster AJ, Tamura T, Baumeister W, (1999) Capsids of tricorn protease studied by electron cryomicroscopy. J Struct Biol 128: 65-68.
    • (1999) J Struct Biol , vol.128 , pp. 65-68
    • Walz, J.1    Koster, A.J.2    Tamura, T.3    Baumeister, W.4
  • 11
    • 13844255627 scopus 로고    scopus 로고
    • Crystal structure of TET protease reveals complementary protein degradation pathways in prokaryotes
    • Borissenko L, Groll M, (2005) Crystal structure of TET protease reveals complementary protein degradation pathways in prokaryotes. J Mol Biol 346: 1207-1219.
    • (2005) J Mol Biol , vol.346 , pp. 1207-1219
    • Borissenko, L.1    Groll, M.2
  • 12
    • 0036565988 scopus 로고    scopus 로고
    • Tetrahedral aminopeptidase: a novel large protease complex from archaea
    • Franzetti B, Schoehn G, Hernandez JF, Jaquinod M, Ruigrok RW, et al.(2002) Tetrahedral aminopeptidase: a novel large protease complex from archaea. EMBO J 21: 2132-2138.
    • (2002) EMBO J , vol.21 , pp. 2132-2138
    • Franzetti, B.1    Schoehn, G.2    Hernandez, J.F.3    Jaquinod, M.4    Ruigrok, R.W.5
  • 13
    • 10944251348 scopus 로고    scopus 로고
    • Crystal structure of a dodecameric tetrahedral-shaped aminopeptidase
    • Russo S, Baumann U, (2004) Crystal structure of a dodecameric tetrahedral-shaped aminopeptidase. J Biol Chem 279: 51275-51281.
    • (2004) J Biol Chem , vol.279 , pp. 51275-51281
    • Russo, S.1    Baumann, U.2
  • 14
    • 33846021304 scopus 로고    scopus 로고
    • An archaeal peptidase assembles into two different quaternary structures: A tetrahedron and a giant octahedron
    • Schoehn G, Vellieux FM, Asuncion Dura M, Receveur-Brechot V, Fabry CM, et al.(2006) An archaeal peptidase assembles into two different quaternary structures: A tetrahedron and a giant octahedron. J Biol Chem 281: 36327-36337.
    • (2006) J Biol Chem , vol.281 , pp. 36327-36337
    • Schoehn, G.1    Vellieux, F.M.2    Asuncion Dura, M.3    Receveur-Brechot, V.4    Fabry, C.M.5
  • 15
    • 22544435789 scopus 로고    scopus 로고
    • Molecular architecture and assembly mechanism of Drosophila tripeptidyl peptidase II
    • Rockel B, Peters J, Muller SA, Seyit G, Ringler P, et al.(2005) Molecular architecture and assembly mechanism of Drosophila tripeptidyl peptidase II. Proc Natl Acad Sci U S A 102: 10135-10140.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 10135-10140
    • Rockel, B.1    Peters, J.2    Muller, S.A.3    Seyit, G.4    Ringler, P.5
  • 16
    • 0034881189 scopus 로고    scopus 로고
    • Structure of the Bacillus subtilis D-aminopeptidase DppA reveals a novel self-compartmentalizing protease
    • Remaut H, Bompard-Gilles C, Goffin C, Frere JM, Van Beeumen J, (2001) Structure of the Bacillus subtilis D-aminopeptidase DppA reveals a novel self-compartmentalizing protease. Nat Struct Biol 8: 674-678.
    • (2001) Nat Struct Biol , vol.8 , pp. 674-678
    • Remaut, H.1    Bompard-Gilles, C.2    Goffin, C.3    Frere, J.M.4    Van Beeumen, J.5
  • 17
    • 0141890963 scopus 로고    scopus 로고
    • High-phasing-power lanthanide derivatives: taking advantage of ytterbium and lutetium for optimized anomalous diffraction experiments using synchrotron radiation
    • Girard E, Anelli PL, Vicat J, Kahn R, (2003) High-phasing-power lanthanide derivatives: taking advantage of ytterbium and lutetium for optimized anomalous diffraction experiments using synchrotron radiation. Acta Crystallogr D Biol Crystallogr 59: 1877-1880.
    • (2003) Acta Crystallogr D Biol Crystallogr , vol.59 , pp. 1877-1880
    • Girard, E.1    Anelli, P.L.2    Vicat, J.3    Kahn, R.4
  • 19
    • 0034684162 scopus 로고    scopus 로고
    • The bacterial lipocalins
    • Bishop RE, (2000) The bacterial lipocalins. Biochim Biophys Acta 1482: 73-83.
    • (2000) Biochim Biophys Acta , vol.1482 , pp. 73-83
    • Bishop, R.E.1
  • 20
    • 0026755238 scopus 로고
    • Archaea in coastal marine environments
    • DeLong EF, (1992) Archaea in coastal marine environments. Proc Natl Acad Sci U S A 89: 5685-5689.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 5685-5689
    • DeLong, E.F.1
  • 21
    • 33846151740 scopus 로고    scopus 로고
    • Biochemical and phylogenetic characterization of a novel terrestrial hyperthermophilic archaeon pertaining to the genus Pyrococcus from an Algerian hydrothermal hot spring
    • Kecha M, Benallaoua S, Touzel JP, Bonaly R, Duchiron F, (2007) Biochemical and phylogenetic characterization of a novel terrestrial hyperthermophilic archaeon pertaining to the genus Pyrococcus from an Algerian hydrothermal hot spring. Extremophiles 11: 65-73.
    • (2007) Extremophiles , vol.11 , pp. 65-73
    • Kecha, M.1    Benallaoua, S.2    Touzel, J.P.3    Bonaly, R.4    Duchiron, F.5
  • 23
    • 33744468540 scopus 로고    scopus 로고
    • Cloning, purification, crystallization and preliminary crystallographic analysis of a penicillin-binding protein homologue from Pyrococcus abyssi
    • Delfosse V, Hugonnet JE, Sougakoff W, Mayer C, (2005) Cloning, purification, crystallization and preliminary crystallographic analysis of a penicillin-binding protein homologue from Pyrococcus abyssi. Acta Crystallogr Sect F Struct Biol Cryst Commun 61: 1006-1008.
    • (2005) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.61 , pp. 1006-1008
    • Delfosse, V.1    Hugonnet, J.E.2    Sougakoff, W.3    Mayer, C.4
  • 25
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
    • Schuck P, (2000) Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. Biophys J 78: 1606-1619.
    • (2000) Biophys J , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 28
    • 0021119424 scopus 로고
    • Three-dimensional reconstruction of imperfect two-dimensional crystals
    • Saxton WO, Baumeister W, Hahn M, (1984) Three-dimensional reconstruction of imperfect two-dimensional crystals. 13: 57-70.
    • (1984) , vol.13 , pp. 57-70
    • Saxton, W.O.1    Baumeister, W.2    Hahn, M.3
  • 30
    • 85027632383 scopus 로고
    • Automatic indexing of rotation diffraction patterns
    • Kabsch W, (1988) Automatic indexing of rotation diffraction patterns. J Appl Cryst 21: 67-71.
    • (1988) J Appl Cryst , vol.21 , pp. 67-71
    • Kabsch, W.1
  • 31
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project 4
    • Collaborative Computational Project 4(1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50: 760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 33
    • 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: 1002-1011.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 1002-1011
    • Cowtan, K.1
  • 34
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K, (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 36
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, Thornton JM, (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Cryst 26: 283-291.
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 37
    • 0348062818 scopus 로고    scopus 로고
    • The SWISS-MODEL Repository of annotated three-dimensional protein structure homology models
    • Kopp J, Schwede T, (2004) The SWISS-MODEL Repository of annotated three-dimensional protein structure homology models. Nucleic Acids Res 32: D230-234.
    • (2004) Nucleic Acids Res , vol.32
    • Kopp, J.1    Schwede, T.2
  • 38
    • 0035175679 scopus 로고    scopus 로고
    • PDBsum: summaries and analyses of PDB structures
    • Laskowski RA, (2001) PDBsum: summaries and analyses of PDB structures. Nucleic Acids Res 29: 221-222.
    • (2001) Nucleic Acids Res , vol.29 , pp. 221-222
    • Laskowski, R.A.1
  • 39
    • 0030767485 scopus 로고    scopus 로고
    • VERIFY3D: assessment of protein models with three-dimensional profiles
    • Eisenberg D, Lüthy R, Bowie JU, (1997) VERIFY3D: assessment of protein models with three-dimensional profiles. Methods in enzymololy 277: 396-404.
    • (1997) Methods in Enzymololy , vol.277 , pp. 396-404
    • Eisenberg, D.1    Lüthy, R.2    Bowie, J.U.3
  • 40
    • 0027490731 scopus 로고
    • Recognition of errors in three-dimensional structures of proteins
    • Sippl MJ, (1993) Recognition of errors in three-dimensional structures of proteins. Proteins 17: 355-362.
    • (1993) Proteins , vol.17 , pp. 355-362
    • Sippl, M.J.1
  • 41
    • 0027145981 scopus 로고
    • Improved alignment of weakly homologous protein sequences using structural information
    • Gracy J, Chiche L, Sallantin J, (1993) Improved alignment of weakly homologous protein sequences using structural information. Protein Engineering, Design and Selection 6: 821-829.
    • (1993) Protein Engineering, Design and Selection , vol.6 , pp. 821-829
    • Gracy, J.1    Chiche, L.2    Sallantin, J.3
  • 42
    • 0021103421 scopus 로고
    • Solution composition dependent variation in extinction coefficients for p-nitroaniline
    • Lottenberg R, Jackson CM, (1983) Solution composition dependent variation in extinction coefficients for p-nitroaniline. Biochim Biophys Acta 742: 558-564.
    • (1983) Biochim Biophys Acta , vol.742 , pp. 558-564
    • Lottenberg, R.1    Jackson, C.M.2
  • 43
    • 4744353202 scopus 로고    scopus 로고
    • Synthesis of mosaic peptidoglycan cross-bridges by hybrid peptidoglycan assembly pathways in gram-positive bacteria
    • Arbeloa A, Hugonnet JE, Sentilhes AC, Josseaume N, Dubost L, et al.(2004) Synthesis of mosaic peptidoglycan cross-bridges by hybrid peptidoglycan assembly pathways in gram-positive bacteria. J Biol Chem 279: 41546-41556.
    • (2004) J Biol Chem , vol.279 , pp. 41546-41556
    • Arbeloa, A.1    Hugonnet, J.E.2    Sentilhes, A.C.3    Josseaume, N.4    Dubost, L.5
  • 44
    • 0015980566 scopus 로고
    • Conjugal transfer of plasmid-borne multiple antibiotic resistance in Streptococcus faecalis var. zymogenes
    • Jacob AE, Hobbs SJ, (1974) Conjugal transfer of plasmid-borne multiple antibiotic resistance in Streptococcus faecalis var. zymogenes. J Bacteriol 117: 360-372.
    • (1974) J Bacteriol , vol.117 , pp. 360-372
    • Jacob, A.E.1    Hobbs, S.J.2
  • 45
    • 0023765918 scopus 로고
    • Separation and quantification of muropeptides with high-performance liquid chromatography
    • Glauner B, (1988) Separation and quantification of muropeptides with high-performance liquid chromatography. Anal Biochem 172: 451-464.
    • (1988) Anal Biochem , vol.172 , pp. 451-464
    • Glauner, B.1
  • 46
    • 0032823023 scopus 로고    scopus 로고
    • Expression of the Staphylococcus aureus UDP-N-acetylmuramoyl- L-alanyl-D-glutamate:L-lysine ligase in Escherichia coli and effects on peptidoglycan biosynthesis and cell growth
    • Mengin-Lecreulx D, Falla T, Blanot D, van Heijenoort J, Adams DJ, et al.(1999) Expression of the Staphylococcus aureus UDP-N-acetylmuramoyl- L-alanyl-D-glutamate:L-lysine ligase in Escherichia coli and effects on peptidoglycan biosynthesis and cell growth. J Bacteriol 181: 5909-5914.
    • (1999) J Bacteriol , vol.181 , pp. 5909-5914
    • Mengin-Lecreulx, D.1    Falla, T.2    Blanot, D.3    van Heijenoort, J.4    Adams, D.J.5


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