메뉴 건너뛰기




Volumn 381, Issue 4, 2008, Pages 867-880

Structural Insights into the Recognition of Peroxisomal Targeting Signal 1 by Trypanosoma brucei Peroxin 5

Author keywords

drug design; glycosomes; peroxisomes; sleeping sickness; TPR motif

Indexed keywords

CYTOSOL RECEPTOR; PEROXISOMAL TARGETING SIGNAL 1 HARBORING PROTEIN; PROTEIN;

EID: 48449100534     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.05.089     Document Type: Article
Times cited : (43)

References (56)
  • 2
    • 48449091218 scopus 로고    scopus 로고
    • WHO (2006). African trypanosomiasis (sleeping sickness). Fact sheet N°259, http://www.who.int/mediacentre/factsheets/fs259/en/.
    • WHO (2006). African trypanosomiasis (sleeping sickness). Fact sheet N°259, http://www.who.int/mediacentre/factsheets/fs259/en/.
  • 3
    • 0035201134 scopus 로고    scopus 로고
    • New drugs for the treatment of human African trypanosomiasis: research and development
    • Keiser J., Stich A., and Burri C. New drugs for the treatment of human African trypanosomiasis: research and development. Trends Parasitol. 17 (2001) 42-49
    • (2001) Trends Parasitol. , vol.17 , pp. 42-49
    • Keiser, J.1    Stich, A.2    Burri, C.3
  • 5
    • 0017366999 scopus 로고
    • Localization of nine glycolytic enzymes in a microbody-like organelle in Trypanosoma brucei: the glycosome
    • Opperdoes F.R., and Borst P. Localization of nine glycolytic enzymes in a microbody-like organelle in Trypanosoma brucei: the glycosome. FEBS Lett. 80 (1977) 360-364
    • (1977) FEBS Lett. , vol.80 , pp. 360-364
    • Opperdoes, F.R.1    Borst, P.2
  • 6
    • 0034333236 scopus 로고    scopus 로고
    • Metabolic aspects of glycosomes in Trypanosomatidae-new data and views
    • Michels P.A., Hannaert V., and Bringaud F. Metabolic aspects of glycosomes in Trypanosomatidae-new data and views. Parasitol. Today 16 (2000) 482-489
    • (2000) Parasitol. Today , vol.16 , pp. 482-489
    • Michels, P.A.1    Hannaert, V.2    Bringaud, F.3
  • 8
    • 7944224890 scopus 로고    scopus 로고
    • Biogenesis of peroxisomes and glycosomes: trypanosomatid glycosome assembly is a promising new drug target
    • Moyersoen J., Choe J., Fan E., Hol W.G., and Michels P.A. Biogenesis of peroxisomes and glycosomes: trypanosomatid glycosome assembly is a promising new drug target. FEMS Microbiol. Rev. 28 (2004) 603-643
    • (2004) FEMS Microbiol. Rev. , vol.28 , pp. 603-643
    • Moyersoen, J.1    Choe, J.2    Fan, E.3    Hol, W.G.4    Michels, P.A.5
  • 9
    • 32144453674 scopus 로고    scopus 로고
    • Sleeping sickness: PEX and drugs
    • Schliebs W. Sleeping sickness: PEX and drugs. Biochim. Biophys. Acta 1763 (2006) 4-5
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 4-5
    • Schliebs, W.1
  • 10
    • 33947301320 scopus 로고    scopus 로고
    • Characterization of the role of the receptors PEX5 and PEX7 in the import of proteins into glycosomes of Trypanosoma brucei
    • Galland N., Demeure F., Hannaert V., Verplaetse E., Vertommen D., Van Der Smissen P., et al. Characterization of the role of the receptors PEX5 and PEX7 in the import of proteins into glycosomes of Trypanosoma brucei. Biochim. Biophys. Acta 1773 (2007) 521-535
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 521-535
    • Galland, N.1    Demeure, F.2    Hannaert, V.3    Verplaetse, E.4    Vertommen, D.5    Van Der Smissen, P.6
  • 11
    • 15744388086 scopus 로고    scopus 로고
    • Probing the role of compartmentation of glycolysis in procyclic form Trypanosoma brucei: RNA interference studies of PEX14, hexokinase, and phosphofructokinase
    • Kessler P.S., and Parsons M. Probing the role of compartmentation of glycolysis in procyclic form Trypanosoma brucei: RNA interference studies of PEX14, hexokinase, and phosphofructokinase. J. Biol. Chem. 280 (2005) 9030-9036
    • (2005) J. Biol. Chem. , vol.280 , pp. 9030-9036
    • Kessler, P.S.1    Parsons, M.2
  • 12
    • 0036273592 scopus 로고    scopus 로고
    • Opinion: peroxisomal-protein import: is it really that complex?
    • Gould S.J., and Collins C.S. Opinion: peroxisomal-protein import: is it really that complex?. Nat. Rev. Mol. Cell Biol. 3 (2002) 382-389
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 382-389
    • Gould, S.J.1    Collins, C.S.2
  • 13
    • 33845318489 scopus 로고    scopus 로고
    • Uniqueness of the mechanism of protein import into the peroxisome matrix: transport of folded, co-factor-bound and oligomeric proteins by shuttling receptors
    • Leon S., Goodman J.M., and Subramani S. Uniqueness of the mechanism of protein import into the peroxisome matrix: transport of folded, co-factor-bound and oligomeric proteins by shuttling receptors. Biochim. Biophys. Acta 1763 (2006) 1552-1564
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 1552-1564
    • Leon, S.1    Goodman, J.M.2    Subramani, S.3
  • 14
    • 27744523622 scopus 로고    scopus 로고
    • Peroxisomal matrix protein import: the transient pore model
    • Erdmann R., and Schliebs W. Peroxisomal matrix protein import: the transient pore model. Nat. Rev. Mol. Cell Biol. 6 (2005) 738-742
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 738-742
    • Erdmann, R.1    Schliebs, W.2
  • 15
    • 33845370951 scopus 로고    scopus 로고
    • The importomer-a peroxisomal membrane complex involved in protein translocation into the peroxisome matrix
    • Rayapuram N., and Subramani S. The importomer-a peroxisomal membrane complex involved in protein translocation into the peroxisome matrix. Biochim. Biophys. Acta 1763 (2006) 1613-1619
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 1613-1619
    • Rayapuram, N.1    Subramani, S.2
  • 17
    • 0035917528 scopus 로고    scopus 로고
    • The human peroxisomal targeting signal receptor, Pex5p, is translocated into the peroxisomal matrix and recycled to the cytosol
    • Dammai V., and Subramani S. The human peroxisomal targeting signal receptor, Pex5p, is translocated into the peroxisomal matrix and recycled to the cytosol. Cell 105 (2001) 187-196
    • (2001) Cell , vol.105 , pp. 187-196
    • Dammai, V.1    Subramani, S.2
  • 18
    • 9444297831 scopus 로고    scopus 로고
    • Pex7p translocates in and out of peroxisomes in Saccharomyces cerevisiae
    • Nair D.M., Purdue P.E., and Lazarow P.B. Pex7p translocates in and out of peroxisomes in Saccharomyces cerevisiae. J. Cell Biol. 167 (2004) 599-604
    • (2004) J. Cell Biol. , vol.167 , pp. 599-604
    • Nair, D.M.1    Purdue, P.E.2    Lazarow, P.B.3
  • 19
    • 34249908934 scopus 로고    scopus 로고
    • The peroxisomal protein import machinery
    • Platta H.W., and Erdmann R. The peroxisomal protein import machinery. FEBS Lett. 581 (2007) 2811-2819
    • (2007) FEBS Lett. , vol.581 , pp. 2811-2819
    • Platta, H.W.1    Erdmann, R.2
  • 21
    • 33845300838 scopus 로고    scopus 로고
    • Peroxisome targeting signal 1: is it really a simple tripeptide?
    • Brocard C., and Hartig A. Peroxisome targeting signal 1: is it really a simple tripeptide?. Biochim. Biophys. Acta 1763 (2006) 1565-1573
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 1565-1573
    • Brocard, C.1    Hartig, A.2
  • 22
    • 2542601506 scopus 로고    scopus 로고
    • Pex5p binding affinities for canonical and noncanonical PTS1 peptides
    • Maynard E.L., Gatto Jr. G.J., and Berg J.M. Pex5p binding affinities for canonical and noncanonical PTS1 peptides. Proteins 55 (2004) 856-861
    • (2004) Proteins , vol.55 , pp. 856-861
    • Maynard, E.L.1    Gatto Jr., G.J.2    Berg, J.M.3
  • 23
    • 0032509362 scopus 로고    scopus 로고
    • The difference in recognition of terminal tripeptides as peroxisomal targeting signal 1 between yeast and human is due to different affinities of their receptor Pex5p to the cognate signal and to residues adjacent to it
    • Lametschwandtner G., Brocard C., Fransen M., Van Veldhoven P., Berger J., and Hartig A. The difference in recognition of terminal tripeptides as peroxisomal targeting signal 1 between yeast and human is due to different affinities of their receptor Pex5p to the cognate signal and to residues adjacent to it. J. Biol. Chem. 273 (1998) 33635-33643
    • (1998) J. Biol. Chem. , vol.273 , pp. 33635-33643
    • Lametschwandtner, G.1    Brocard, C.2    Fransen, M.3    Van Veldhoven, P.4    Berger, J.5    Hartig, A.6
  • 24
    • 0037414447 scopus 로고    scopus 로고
    • Motif refinement of the peroxisomal targeting signal 1 and evaluation of taxon-specific differences
    • Neuberger G., Maurer-Stroh S., Eisenhaber B., Hartig A., and Eisenhaber F. Motif refinement of the peroxisomal targeting signal 1 and evaluation of taxon-specific differences. J. Mol. Biol. 328 (2003) 567-579
    • (2003) J. Mol. Biol. , vol.328 , pp. 567-579
    • Neuberger, G.1    Maurer-Stroh, S.2    Eisenhaber, B.3    Hartig, A.4    Eisenhaber, F.5
  • 25
    • 0032473425 scopus 로고    scopus 로고
    • The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions
    • Das A.K., Cohen P.W., and Barford D. The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions. EMBO J. 17 (1998) 1192-1199
    • (1998) EMBO J. , vol.17 , pp. 1192-1199
    • Das, A.K.1    Cohen, P.W.2    Barford, D.3
  • 26
    • 0344628648 scopus 로고    scopus 로고
    • TPR proteins: the versatile helix
    • D'Andrea L.D., and Regan L. TPR proteins: the versatile helix. Trends Biochem. Sci. 28 (2003) 655-662
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 655-662
    • D'Andrea, L.D.1    Regan, L.2
  • 27
    • 0344496513 scopus 로고    scopus 로고
    • The tetratricopeptide repeat: a structural motif mediating protein-protein interactions
    • Blatch G.L., and Lassle M. The tetratricopeptide repeat: a structural motif mediating protein-protein interactions. BioEssays 21 (1999) 932-939
    • (1999) BioEssays , vol.21 , pp. 932-939
    • Blatch, G.L.1    Lassle, M.2
  • 28
    • 0033664345 scopus 로고    scopus 로고
    • Peroxisomal targeting signal-1 recognition by the TPR domains of human PEX5
    • Gatto Jr. G.J., Geisbrecht B.V., Gould S.J., and Berg J.M. Peroxisomal targeting signal-1 recognition by the TPR domains of human PEX5. Nat. Struct. Biol. 7 (2000) 1091-1095
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1091-1095
    • Gatto Jr., G.J.1    Geisbrecht, B.V.2    Gould, S.J.3    Berg, J.M.4
  • 29
    • 33751545341 scopus 로고    scopus 로고
    • Recognition of a functional peroxisome type 1 target by the dynamic import receptor Pex5p
    • Stanley W.A., Filipp F.V., Kursula P., Schuller N., Erdmann R., Schliebs W., et al. Recognition of a functional peroxisome type 1 target by the dynamic import receptor Pex5p. Mol. Cell 24 (2006) 653-663
    • (2006) Mol. Cell , vol.24 , pp. 653-663
    • Stanley, W.A.1    Filipp, F.V.2    Kursula, P.3    Schuller, N.4    Erdmann, R.5    Schliebs, W.6
  • 30
    • 34247348088 scopus 로고    scopus 로고
    • A previously unobserved conformation for the human Pex5p receptor suggests roles for intrinsic flexibility and rigid domain motions in ligand binding
    • Stanley W.A., Pursiainen N.V., Garman E.F., Juffer A.H., Wilmanns M., and Kursula P. A previously unobserved conformation for the human Pex5p receptor suggests roles for intrinsic flexibility and rigid domain motions in ligand binding. BMC Struct. Biol. 7 (2007) 24
    • (2007) BMC Struct. Biol. , vol.7 , pp. 24
    • Stanley, W.A.1    Pursiainen, N.V.2    Garman, E.F.3    Juffer, A.H.4    Wilmanns, M.5    Kursula, P.6
  • 31
    • 33845321747 scopus 로고    scopus 로고
    • Dynamic architecture of the peroxisomal import receptor Pex5p
    • Stanley W.A., and Wilmanns M. Dynamic architecture of the peroxisomal import receptor Pex5p. Biochim. Biophys. Acta 1763 (2006) 1592-1598
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 1592-1598
    • Stanley, W.A.1    Wilmanns, M.2
  • 33
    • 0035896043 scopus 로고    scopus 로고
    • An unexpected extended conformation for the third TPR motif of the peroxin PEX5 from Trypanosoma brucei
    • Kumar A., Roach C., Hirsh I.S., Turley S., de Walque S., Michels P.A., and Hol W.G. An unexpected extended conformation for the third TPR motif of the peroxin PEX5 from Trypanosoma brucei. J. Mol. Biol. 307 (2001) 271-282
    • (2001) J. Mol. Biol. , vol.307 , pp. 271-282
    • Kumar, A.1    Roach, C.2    Hirsh, I.S.3    Turley, S.4    de Walque, S.5    Michels, P.A.6    Hol, W.G.7
  • 34
  • 35
  • 36
    • 34948828119 scopus 로고    scopus 로고
    • Protein translocation into peroxisomes by ring-shaped import receptors
    • Stanley W.A., Fodor K., Marti-Renom M.A., Schliebs W., and Wilmanns M. Protein translocation into peroxisomes by ring-shaped import receptors. FEBS Lett. 581 (2007) 4795-4802
    • (2007) FEBS Lett. , vol.581 , pp. 4795-4802
    • Stanley, W.A.1    Fodor, K.2    Marti-Renom, M.A.3    Schliebs, W.4    Wilmanns, M.5
  • 37
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-Structure Matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E., and Henrick K. Secondary-Structure Matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr., Sect. D: Biol. Crystallogr. 60 (2004) 2256-2268
    • (2004) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 39
    • 0026055156 scopus 로고
    • Analysis of the steric strain in the polypeptide backbone of protein molecules
    • Herzberg O., and Moult J. Analysis of the steric strain in the polypeptide backbone of protein molecules. Proteins 11 (1991) 223-229
    • (1991) Proteins , vol.11 , pp. 223-229
    • Herzberg, O.1    Moult, J.2
  • 41
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • Scheufler C., Brinker A., Bourenkov G., Pegoraro S., Moroder L., Bartunik H., et al. Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 101 (2000) 199-210
    • (2000) Cell , vol.101 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6
  • 43
    • 33747818007 scopus 로고    scopus 로고
    • CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues
    • Dundas J., Ouyang Z., Tseng J., Binkowski A., Turpaz Y., and Liang J. CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues. Nucleic Acids Res. 34 (2006) W116-W118
    • (2006) Nucleic Acids Res. , vol.34
    • Dundas, J.1    Ouyang, Z.2    Tseng, J.3    Binkowski, A.4    Turpaz, Y.5    Liang, J.6
  • 44
    • 0030151990 scopus 로고    scopus 로고
    • Site-directed mutagenesis techniques in the study of Escherichia coli serine hydroxymethyltransferase
    • Iurescia S., Condo I., Angelaccio S., Delle Fratte S., and Bossa F. Site-directed mutagenesis techniques in the study of Escherichia coli serine hydroxymethyltransferase. Protein Expression Purif. 7 (1996) 323-328
    • (1996) Protein Expression Purif. , vol.7 , pp. 323-328
    • Iurescia, S.1    Condo, I.2    Angelaccio, S.3    Delle Fratte, S.4    Bossa, F.5
  • 46
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Carter C., and Sweet R. (Eds), Academic Press, New York
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. In: Carter C., and Sweet R. (Eds). Methods in Enzymology vol. 276 (1997), Academic Press, New York 307-326
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 50
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project, No. 4
    • Collaborative Computational Project, No. 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr., Sect. D: Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , pp. 760-763
  • 52
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • Painter J., and Merritt E.A. Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr., Sect. D: Biol. Crystallogr. 62 (2006) 439-450
    • (2006) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.62 , pp. 439-450
    • Painter, J.1    Merritt, E.A.2
  • 53
    • 33645158291 scopus 로고    scopus 로고
    • TLSMD web server for the generation of multi-group TLS models
    • Painter J., and Merritt E.A. TLSMD web server for the generation of multi-group TLS models. J. Appl. Crystallogr. 39 (2006) 109-111
    • (2006) J. Appl. Crystallogr. , vol.39 , pp. 109-111
    • Painter, J.1    Merritt, E.A.2
  • 54
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A., and Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30 (1997) 1022-1025
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 55
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A., Morris R., and Lamzin V.S. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6 (1999) 458-463
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 56
    • 48449092704 scopus 로고    scopus 로고
    • DeLano, W. L. (2002). The PyMOL Molecular Graphics System. http://pymol.sourceforge.net.
    • DeLano, W. L. (2002). The PyMOL Molecular Graphics System. http://pymol.sourceforge.net.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.