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Volumn 1804, Issue 7, 2010, Pages 1537-1541

Restricted domain mobility in the Candida albicans Ess1 prolyl isomerase

Author keywords

15N relaxation; Chemical shift; Domain; Flexibility; NMR; Prolyl isomerase

Indexed keywords

ISOMERASE; PEPTIDYLPROLYL ISOMERASE PIN1; PROTEIN ESS1; UNCLASSIFIED DRUG;

EID: 77952323518     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2010.03.005     Document Type: Article
Times cited : (4)

References (36)
  • 1
    • 0024540118 scopus 로고
    • Sequence and mutational analysis of ESS1, a gene essential for growth in Saccharomyces cerevisiae
    • Hanes S.D., Shank P.R., and Bostian K.A. Sequence and mutational analysis of ESS1, a gene essential for growth in Saccharomyces cerevisiae. Yeast 5 (1989) 55-72
    • (1989) Yeast , vol.5 , pp. 55-72
    • Hanes, S.D.1    Shank, P.R.2    Bostian, K.A.3
  • 2
    • 0032951711 scopus 로고    scopus 로고
    • Mutations in a peptidylprolyl-cis/trans-isomerase gene lead to a defect in 3'-end formation of a pre-mRNA in Saccharomyces cerevisiae
    • Hani J., Schelbert B., Bernhardt A., Domdey H., Fischer G., Wiebauer K., and Rahfeld J.U. Mutations in a peptidylprolyl-cis/trans-isomerase gene lead to a defect in 3'-end formation of a pre-mRNA in Saccharomyces cerevisiae. J. Biol. Chem. 274 (1999) 108-116
    • (1999) J. Biol. Chem. , vol.274 , pp. 108-116
    • Hani, J.1    Schelbert, B.2    Bernhardt, A.3    Domdey, H.4    Fischer, G.5    Wiebauer, K.6    Rahfeld, J.U.7
  • 4
    • 0033615705 scopus 로고    scopus 로고
    • Phospho-carboxyl-terminal domain binding and the role of a prolyl isomerase in pre-mRNA 3′-end formation
    • Morris D.P., Phatnani H.P., and Greenleaf A.L. Phospho-carboxyl-terminal domain binding and the role of a prolyl isomerase in pre-mRNA 3′-end formation. J. Biol. Chem. 274 (1999) 31583-31587
    • (1999) J. Biol. Chem. , vol.274 , pp. 31583-31587
    • Morris, D.P.1    Phatnani, H.P.2    Greenleaf, A.L.3
  • 5
    • 17644413069 scopus 로고    scopus 로고
    • Vanishingly low levels of Ess1 prolyl-isomerase activity are sufficient for growth in Saccharomyces cerevisiae
    • Gemmill T.R., Wu X., and Hanes S.D. Vanishingly low levels of Ess1 prolyl-isomerase activity are sufficient for growth in Saccharomyces cerevisiae. J. Biol. Chem. 280 (2005) 15510-15517
    • (2005) J. Biol. Chem. , vol.280 , pp. 15510-15517
    • Gemmill, T.R.1    Wu, X.2    Hanes, S.D.3
  • 7
    • 1842763560 scopus 로고    scopus 로고
    • Pinning down cell signaling, cancer and Alzheimer's disease
    • Lu K.P. Pinning down cell signaling, cancer and Alzheimer's disease. Trends Biochem. Sci. 29 (2004) 200-209
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 200-209
    • Lu, K.P.1
  • 9
    • 0036165610 scopus 로고    scopus 로고
    • The Ess1 prolyl isomerase is required for growth and morphogenetic switching in Candida albicans
    • Devasahayam G., Chaturvedi V., and Hanes S.D. The Ess1 prolyl isomerase is required for growth and morphogenetic switching in Candida albicans. Genetics 160 (2002) 37-48
    • (2002) Genetics , vol.160 , pp. 37-48
    • Devasahayam, G.1    Chaturvedi, V.2    Hanes, S.D.3
  • 10
    • 17644406232 scopus 로고    scopus 로고
    • The Ess1 prolyl isomerase is dispensible for growth but required for virulence in Cryptococcus neoformans
    • Ren P., Chaturvedi V., and Hanes S.D. The Ess1 prolyl isomerase is dispensible for growth but required for virulence in Cryptococcus neoformans. Microbiology 151 (2005) 1593-1605
    • (2005) Microbiology , vol.151 , pp. 1593-1605
    • Ren, P.1    Chaturvedi, V.2    Hanes, S.D.3
  • 12
    • 62749128097 scopus 로고    scopus 로고
    • Recent approaches to antifungal therapy for invasive mycoses
    • Mathew B.P., and Nath M. Recent approaches to antifungal therapy for invasive mycoses. ChemMedChem 4 (2009) 310-323
    • (2009) ChemMedChem , vol.4 , pp. 310-323
    • Mathew, B.P.1    Nath, M.2
  • 13
    • 3242703074 scopus 로고    scopus 로고
    • Toward more effective antifungal therapy: the prospects of combination therapy
    • Kontoyiannis D.P., and Lewis R.E. Toward more effective antifungal therapy: the prospects of combination therapy. Br. J. Haematol. 126 (2004) 165-175
    • (2004) Br. J. Haematol. , vol.126 , pp. 165-175
    • Kontoyiannis, D.P.1    Lewis, R.E.2
  • 14
    • 0008233581 scopus 로고    scopus 로고
    • Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent
    • Ranganathan R., Lu K.P., Hunter T., and Noel J.P. Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent. Cell 89 (1997) 875-886
    • (1997) Cell , vol.89 , pp. 875-886
    • Ranganathan, R.1    Lu, K.P.2    Hunter, T.3    Noel, J.P.4
  • 15
    • 0033885803 scopus 로고    scopus 로고
    • Structural basis for phosphoserine-proline recognition by group IV WW domains
    • Verdecia M.A., Bowman M.E., Lu K.P., Hunter T., and Noel J.P. Structural basis for phosphoserine-proline recognition by group IV WW domains. Nat. Struct. Biol. 7 (2000) 639-643
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 639-643
    • Verdecia, M.A.1    Bowman, M.E.2    Lu, K.P.3    Hunter, T.4    Noel, J.P.5
  • 16
    • 0038342514 scopus 로고    scopus 로고
    • Peptide binding induces large scale changes in inter-domain mobility in human Pin1
    • Jacobs D.M., Saxena K., Vogherr M., Bernado P., Pons M., and Fiebig K.M. Peptide binding induces large scale changes in inter-domain mobility in human Pin1. J. Biol. Chem. 278 (2003) 26174-26182
    • (2003) J. Biol. Chem. , vol.278 , pp. 26174-26182
    • Jacobs, D.M.1    Saxena, K.2    Vogherr, M.3    Bernado, P.4    Pons, M.5    Fiebig, K.M.6
  • 17
    • 0038448924 scopus 로고    scopus 로고
    • Structural analysis of the mitotic regulator hPin1 in solution: insights into domain architecture and substrate binding
    • Bayer E., Goettsch S., Mueller J.W., Griewel B., Guiberman E., Mayr L.M., and Bayer P. Structural analysis of the mitotic regulator hPin1 in solution: insights into domain architecture and substrate binding. J. Biol. Chem. 278 (2003) 26183-26193
    • (2003) J. Biol. Chem. , vol.278 , pp. 26183-26193
    • Bayer, E.1    Goettsch, S.2    Mueller, J.W.3    Griewel, B.4    Guiberman, E.5    Mayr, L.M.6    Bayer, P.7
  • 18
    • 17644385551 scopus 로고    scopus 로고
    • The structure of the Candida albicans Ess1 prolyl isomerase reveals a well-ordered linker that restricts domain mobility
    • Li Z., Li H., Devasahayam G., Gemmill T., Chaturvedi V., Hanes S.D., and VanRoey P. The structure of the Candida albicans Ess1 prolyl isomerase reveals a well-ordered linker that restricts domain mobility. Biochemistry 44 (2005) 6180-6189
    • (2005) Biochemistry , vol.44 , pp. 6180-6189
    • Li, Z.1    Li, H.2    Devasahayam, G.3    Gemmill, T.4    Chaturvedi, V.5    Hanes, S.D.6    VanRoey, P.7
  • 19
    • 35348982265 scopus 로고    scopus 로고
    • On the benefit of bivalency in peptide Ligand/Pin1 interactions
    • Daum S., Lücke C., Wildemann D., and Schiene-Fischer C. On the benefit of bivalency in peptide Ligand/Pin1 interactions. J. Mol. Biol. 374 (2007) 147-161
    • (2007) J. Mol. Biol. , vol.374 , pp. 147-161
    • Daum, S.1    Lücke, C.2    Wildemann, D.3    Schiene-Fischer, C.4
  • 23
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme
    • Mandel A.M., Akke M., and Palmer I.A.G. Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme. J. Mol. Biol. 246 (1995) 144-163
    • (1995) J. Mol. Biol. , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer, I.A.G.3
  • 24
    • 0033614004 scopus 로고    scopus 로고
    • Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation
    • Word J.M., Lovell S.C., Richardson J.S., and Richardson D.C. Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation. J. Mol. Biol. 285 (1999) 1733-1747
    • (1999) J. Mol. Biol. , vol.285 , pp. 1733-1747
    • Word, J.M.1    Lovell, S.C.2    Richardson, J.S.3    Richardson, D.C.4
  • 25
    • 0028393784 scopus 로고
    • The 13C Chemical-Shift Index: a simple method for the identification of protein secondary structure using 13C chemical-shift data
    • Wishart D.S., and Sykes B.D. The 13C Chemical-Shift Index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J. Biomolec. NMR 4 (1994) 171-180
    • (1994) J. Biomolec. NMR , vol.4 , pp. 171-180
    • Wishart, D.S.1    Sykes, B.D.2
  • 26
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G., Delaglio F., and Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomolec. NMR 13 (1999) 289-302
    • (1999) J. Biomolec. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 30
    • 0027817195 scopus 로고
    • Mechanism of enzymatic and non-enzymatic prolyl cis-trans isomerization
    • Stein R.L. Mechanism of enzymatic and non-enzymatic prolyl cis-trans isomerization. Adv. Prot. Chem. 44 (1993) 1-24
    • (1993) Adv. Prot. Chem. , vol.44 , pp. 1-24
    • Stein, R.L.1
  • 31
    • 0027742843 scopus 로고
    • A mechanism for rotamase catalysis by the FK506 binding protein (FKBP)
    • Fischer S., Michnick S., and Karplus M. A mechanism for rotamase catalysis by the FK506 binding protein (FKBP). Biochemistry 32 (1993) 13830-13837
    • (1993) Biochemistry , vol.32 , pp. 13830-13837
    • Fischer, S.1    Michnick, S.2    Karplus, M.3
  • 32
    • 0035715945 scopus 로고    scopus 로고
    • Prolyl isomerases
    • Schmid F.X. Prolyl isomerases. Adv. Prot. Chem. 59 (2001) 243-282
    • (2001) Adv. Prot. Chem. , vol.59 , pp. 243-282
    • Schmid, F.X.1
  • 33
    • 0141502348 scopus 로고    scopus 로고
    • Characterization of the overall and local dynamics of a protein with intermediate rotational anisotropy: differentiating between conformational exchange and anisotropic diffusion in the B3 domain of protein G
    • Hall J.B., and Fushman D. Characterization of the overall and local dynamics of a protein with intermediate rotational anisotropy: differentiating between conformational exchange and anisotropic diffusion in the B3 domain of protein G. J. Biomol. NMR 27 (2003) 261-275
    • (2003) J. Biomol. NMR , vol.27 , pp. 261-275
    • Hall, J.B.1    Fushman, D.2
  • 34
    • 34247180580 scopus 로고    scopus 로고
    • Sequence-specific dynamics modulate recognition specificity in WW domains
    • Peng T., Zintsmaster J.S., Namanja A.T., and Peng J.W. Sequence-specific dynamics modulate recognition specificity in WW domains. Nat. Struct. Mol. Biol. 14 (2007) 325-331
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 325-331
    • Peng, T.1    Zintsmaster, J.S.2    Namanja, A.T.3    Peng, J.W.4
  • 36
    • 53149141784 scopus 로고    scopus 로고
    • Structural characterisation of PinA WW domain and a comparison with other Group IV WW domains, Pin1 and Ess1
    • Ng C.A., Kato Y., Tanokura M., and Brownlee R.T.C. Structural characterisation of PinA WW domain and a comparison with other Group IV WW domains, Pin1 and Ess1. Biochim. Biophys. Acta 1784 (2008) 1208-1214
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 1208-1214
    • Ng, C.A.1    Kato, Y.2    Tanokura, M.3    Brownlee, R.T.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.