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Volumn 288, Issue 24, 2013, Pages 17884-17894

A self-compartmentalizing hexamer serine protease from Pyrococcus Horikoshii: Substrate selection achieved through multimerization

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; MONOMERS;

EID: 84879062608     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.451534     Document Type: Article
Times cited : (19)

References (64)
  • 1
    • 41949135032 scopus 로고    scopus 로고
    • Structure, function and biological relevance of prolyl oligopeptidase
    • Szeltner, Z., and Polgár L. (2008) Structure, function and biological relevance of prolyl oligopeptidase. Curr. Protein Pept. Sci. 9, 96-107
    • (2008) Curr. Protein Pept. Sci. , vol.9 , pp. 96-107
    • Szeltner, Z.1    Polgár, L.2
  • 2
    • 0036178438 scopus 로고    scopus 로고
    • The prolyl oligopeptidase family
    • Polgár, L. (2002) The prolyl oligopeptidase family. Cell Mol. Life Sci. 59, 349-362
    • (2002) Cell Mol. Life Sci. , vol.59 , pp. 349-362
    • Polgár, L.1
  • 3
    • 0032563162 scopus 로고    scopus 로고
    • Prolyl oligopeptidase. An unusual β-propeller domain regulates proteolysis
    • Fülöp, V., Böcskei, Z., and Polgár, L. (1998) Prolyl oligopeptidase. An unusual β-propeller domain regulates proteolysis. Cell 94, 161-170
    • (1998) Cell , vol.94 , pp. 161-170
    • Fülöp, V.1    Böcskei, Z.2    Polgár, L.3
  • 4
    • 0037044875 scopus 로고    scopus 로고
    • Electrostatic effects and binding determinants in the catalysis of prolyl oligopeptidase: Site-specific mutagenesis at the oxyanion binding site
    • DOI 10.1074/jbc.M208043200
    • Szeltner, Z., Rea, D., Renner, V., Fulop, V., and Polgar, L. (2002) Electrostatic effects and binding determinants in the catalysis of prolyl oligopeptidase. Site-specific mutagenesis at the oxyanion binding site. J. Biol. Chem. 277, 42613-42622 (Pubitemid 35291120)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.45 , pp. 42613-42622
    • Szeltner, Z.1    Rea, D.2    Renner, V.3    Fulop, V.4    Polgar, L.5
  • 5
    • 0001603385 scopus 로고    scopus 로고
    • Crystal structure of carboxylesterase from Pseudomonas fluorescens, an α/β hydrolase with broad substrate specificity
    • Kim, K. K., Song, H. K., Shin, D. H., Hwang, K. Y., Choe, S., Yoo, O. J., and Suh, S. W. (1997) Crystal structure of carboxylesterase from Pseudomonas fluorescens, an α/β hydrolase with broad substrate specificity. Structure 5, 1571-1584 (Pubitemid 28051972)
    • (1997) Structure , vol.5 , Issue.12 , pp. 1571-1584
    • Kim, K.K.1    Song, H.K.2    Shin, D.H.3    Hwang, K.Y.4    Choe, S.5    Yoo, O.J.6    Suh, S.W.7
  • 6
    • 77954367132 scopus 로고    scopus 로고
    • Induced-fit mechanism for prolyl endopeptidase
    • Li, M., Chen, C., Davies, D. R., and Chiu, T. K. (2010) Induced-fit mechanism for prolyl endopeptidase. J. Biol. Chem. 285, 21487-21495
    • (2010) J. Biol. Chem. , vol.285 , pp. 21487-21495
    • Li, M.1    Chen, C.2    Davies, D.R.3    Chiu, T.K.4
  • 7
    • 14844366112 scopus 로고    scopus 로고
    • Structural and mechanistic analysis of two prolyl endopeptidases: Role of interdomain dynamics in catalysis and specificity
    • DOI 10.1073/pnas.0408286102
    • Shan, L., Mathews, I. I., and Khosla, C. (2005) Structural and mechanistic analysis of two prolyl endopeptidases. Role of interdomain dynamics in catalysis and specificity. Proc. Natl. Acad. Sci. U.S.A. 102, 3599-3604 (Pubitemid 40354657)
    • (2005) Proceedings of the National Academy of Sciences of the United States of America , vol.102 , Issue.10 , pp. 3599-3604
    • Shan, L.1    Mathews, I.I.2    Khosla, C.3
  • 10
    • 29144522905 scopus 로고    scopus 로고
    • Rigidity and flexibility of dipeptidyl peptidase IV: Crystal structures of and docking experiments with DPIV
    • DOI 10.1016/j.jmb.2005.11.014, PII S0022283605014002
    • Engel, M., Hoffmann, T., Manhart, S., Heiser, U., Chambre, S., Huber, R., Demuth, H. U., and Bode, W. (2006) Rigidity and flexibility of dipeptidyl peptidase IV. Crystal structures of and docking experiments with DPIV. J. Mol. Biol. 355, 768-783 (Pubitemid 41817635)
    • (2006) Journal of Molecular Biology , vol.355 , Issue.4 , pp. 768-783
    • Engel, M.1    Hoffmann, T.2    Manhart, S.3    Heiser, U.4    Chambre, S.5    Huber, R.6    Demuth, H.-U.7    Bode, W.8
  • 12
    • 1642534610 scopus 로고    scopus 로고
    • Crystal structure of human dipeptidyl peptidase IV in complex with a decapeptide reveals details on substrate specificity and tetrahedral intermediate formation
    • DOI 10.1110/ps.03460604
    • Aertgeerts, K., Ye, S., Tennant, M. G., Kraus, M. L., Rogers, J., Sang, B. C., Skene, R. J., Webb, D. R., and Prasad, G. S. (2004) Crystal structure of human dipeptidyl peptidase IV in complex with a decapeptide reveals details on substrate specificity and tetrahedral intermediate formation. Protein Sci. 13, 412-421 (Pubitemid 38124962)
    • (2004) Protein Science , vol.13 , Issue.2 , pp. 412-421
    • Aertgeerts, K.1    Ye, S.2    Tennant, M.G.3    Kraus, M.L.4    Rogers, J.5    Sang, B.-C.6    Skene, R.J.7    Webb, D.R.8    Prasad, G.S.9
  • 13
    • 67349149206 scopus 로고    scopus 로고
    • Characterization of a novel acylaminoacyl peptidase with hexameric structure and endopeptidase activity
    • Szeltner, Z., Kiss, A. L., Domokos, K., Harmat, V., Náray- Szabó, G., and Polgár, L. (2009) Characterization of a novel acylaminoacyl peptidase with hexameric structure and endopeptidase activity. Biochim. Biophys. Acta 1794, 1204-1210
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 1204-1210
    • Szeltner, Z.1    Kiss, A.L.2    Domokos, K.3    Harmat, V.4    Náray-Szabó, G.5    Polgár, L.6
  • 14
    • 0028983898 scopus 로고
    • Crystal structure of a conserved protease that binds DNA. The bleomycin hydrolase, Gal6
    • Joshua-Tor, L., Xu, H. E., Johnston, S. A., and Rees, D. C. (1995) Crystal structure of a conserved protease that binds DNA. The bleomycin hydrolase, Gal6. Science 269, 945-950
    • (1995) Science , vol.269 , pp. 945-950
    • Joshua-Tor, L.1    Xu, H.E.2    Johnston, S.A.3    Rees, D.C.4
  • 15
    • 0037073487 scopus 로고    scopus 로고
    • Navigation inside a protease: Substrate selection and product exit in the tricorn protease from Thermoplasma acidophilum
    • DOI 10.1016/S0022-2836(02)01153-1
    • Kim, J. S., Groll, M., Musiol, H. J., Behrendt, R., Kaiser, M., Moroder, L., Huber, R., and Brandstetter, H. (2002) Navigation inside a protease. Substrate selection and product exit in the tricorn protease from Thermoplasma acidophilum. J. Mol. Biol. 324, 1041-1050 (Pubitemid 41782992)
    • (2002) Journal of Molecular Biology , vol.324 , Issue.5 , pp. 1041-1050
    • Kim, J.-S.1    Groll, M.2    Musiol, H.-J.3    Behrendt, R.4    Kaiser, M.5    Moroder, L.6    Huber, R.7    Brandstetter, H.8
  • 17
    • 33947724046 scopus 로고    scopus 로고
    • The Acylaminoacyl Peptidase from Aeropyrum pernix K1 Thought to Be an Exopeptidase Displays Endopeptidase Activity
    • DOI 10.1016/j.jmb.2007.02.025, PII S0022283607002069
    • Kiss, A. L., Hornung, B., Rádi, K., Gengeliczki, Z., Sztáray, B., Juhász, T., Szeltner, Z., Harmat, V., and Polgár L. (2007) The acylaminoacyl peptidase from Aeropyrum pernix K1 thought to be an exopeptidase displays endopeptidase activity. J. Mol. Biol. 368, 509-520 (Pubitemid 46505147)
    • (2007) Journal of Molecular Biology , vol.368 , Issue.2 , pp. 509-520
    • Kiss, A.L.1    Hornung, B.2    Radi, K.3    Gengeliczki, Z.4    Sztaray, B.5    Juhasz, T.6    Szeltner, Z.7    Harmat, V.8    Polgar, L.9
  • 19
    • 0024652794 scopus 로고
    • The DNF15S2 locus at 3p21 is transcribed in normal lung and small cell lung cancer
    • Naylor, S. L., Marshall, A., Hensel, C., Martinez, P. F., Holley, B., and Sakaguchi, A. Y. (1989) The DNF15S2 locus at 3p21 is transcribed in normal lung and small cell lung cancer. Genomics 4, 355-361
    • (1989) Genomics , vol.4 , pp. 355-361
    • Naylor, S.L.1    Marshall, A.2    Hensel, C.3    Martinez, P.F.4    Holley, B.5    Sakaguchi, A.Y.6
  • 21
    • 0025830891 scopus 로고
    • The gene from the short arm of chromosome 3, at D3F15S2, frequently deleted in renal cell carcinoma, encodes acylpeptide hydrolase
    • Erlandsson, R., Boldog, F., Persson, B., Zabarovsky, E. R., Allikmets, R. L., Sümegi, J., Klein, G., and Jörnvall, H. (1991) The gene from the short arm of chromosome 3, at D3F15S2, frequently deleted in renal cell carcinoma, encodes acylpeptide hydrolase. Oncogene 6, 1293-1295 (Pubitemid 21924221)
    • (1991) Oncogene , vol.6 , Issue.7 , pp. 1293-1295
    • Erlandsson, R.1    Boldog, F.2    Persson, B.3    Zabarovsky, E.R.4    Allikmets, R.L.5    Sumegi, J.6    Klein, G.7    Jornvall, H.8
  • 23
    • 0033851169 scopus 로고    scopus 로고
    • Identification of acylpeptide hydrolase as a sensitive site for reaction with organophosphorus compounds and a potential target for cognitive enhancing drugs
    • Richards, P. G., Johnson, M. K., and Ray, D. E. (2000) Identification of acylpeptide hydrolase as a sensitive site for reaction with organophosphorus compounds and a potential target for cognitive enhancing drugs. Mol. Pharmacol. 58, 577-583
    • (2000) Mol. Pharmacol. , vol.58 , pp. 577-583
    • Richards, P.G.1    Johnson, M.K.2    Ray, D.E.3
  • 25
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • Sheldrick, G. M. (2008) A short history of SHELX. Acta Crystallogr. A 64, 112-122
    • (2008) Acta Crystallogr. A , vol.64 , pp. 112-122
    • Sheldrick, G.M.1
  • 26
    • 0002634621 scopus 로고
    • (Wolf, W., Evans, P. R., and Leslie, A. G. W., eds) Daresbury Laboratory, Warrington, UK
    • Otwinowski, Z. (1991) in Proceedings of the CCP4 Study Weekend (Wolf, W., Evans, P. R., and Leslie, A. G. W., eds) pp. 80-86, Daresbury Laboratory, Warrington, UK
    • (1991) Proceedings of the CCP4 Study Weekend , pp. 80-86
    • Otwinowski, Z.1
  • 27
    • 0028103275 scopus 로고
    • The CCP4 suite. Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite. Programs for protein crystallography. Acta Crystallogr. D 50, 760-763
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 28
    • 33748337934 scopus 로고    scopus 로고
    • The Buccaneer software for automated model building
    • Cowtan, K. (2006) The Buccaneer software for automated model building. Acta Crystallogr. D 62, 1002-1011
    • (2006) Acta Crystallogr. D , vol.62 , pp. 1002-1011
    • Cowtan, K.1
  • 29
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An Automated Program for Molecular Replacement
    • Vagin, A., and Teplyakov, A. (1997) MOLREP. An automated program for molecular replacement. J. Appl. Crystallogr. 30, 1022-1025 (Pubitemid 127485985)
    • (1997) Journal of Applied Crystallography , vol.30 , Issue.6 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 33
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • Vaguine, A. A., Richelle, J., and Wodak, S. J. (1999) SFCHECK. A unified set of procedures for evaluating the quality of macromolecular structurefactor data and their agreement with the atomic model. Acta Crystallogr. D 55, 191-205 (Pubitemid 29053816)
    • (1999) Acta Crystallographica Section D: Biological Crystallography , vol.55 , Issue.1 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 35
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4. Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess, B., Kutzner, C., van der Spoel, D., and Lindahl, E. (2008) GROMACS 4. Algorithms for highly efficient, load-balanced, and scalable molecular simulation. J. Chem. Theory Comput. 4, 435-447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 36
    • 3142714765 scopus 로고    scopus 로고
    • Extending the treatment of backbone energetics in protein force fields. Limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations
    • Mackerell, A. D., Jr., Feig, M., and Brooks, C. L., 3rd (2004) Extending the treatment of backbone energetics in protein force fields. Limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations. J. Comput. Chem. 25, 1400-1415
    • (2004) J. Comput. Chem. , vol.25 , pp. 1400-1415
    • Mackerell Jr., A.D.1    Feig, M.2    Brooks III, C.L.3
  • 37
    • 77950106854 scopus 로고    scopus 로고
    • Implementation of the CHARMM force field in GROMACS. Analysis of protein stability effects from correction maps, virtual interaction sites, and water models
    • Bjelkmar, P., Larsson, P., Cuendet, M. A., Hess, B., and Lindahl, E. (2010) Implementation of the CHARMM force field in GROMACS. Analysis of protein stability effects from correction maps, virtual interaction sites, and water models. J. Chem. Theory Comput. 6, 459-466
    • (2010) J. Chem. Theory Comput. , vol.6 , pp. 459-466
    • Bjelkmar, P.1    Larsson, P.2    Cuendet, M.A.3    Hess, B.4    Lindahl, E.5
  • 39
    • 14844366112 scopus 로고    scopus 로고
    • Structural and mechanistic analysis of two endopeptidases. Role of interdomain dynamics in catalysis and specifity
    • Shan, L., Mathews, I. I., and Khosla, C. (2005) Structural and mechanistic analysis of two endopeptidases. Role of interdomain dynamics in catalysis and specifity. Proc. Natl. Acad. Sci. U.S.A. 102, 3599-30604
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 3599-30604
    • Shan, L.1    Mathews, I.I.2    Khosla, C.3
  • 40
    • 78649901973 scopus 로고    scopus 로고
    • Crystal stucture of Leishmania major oligopeptidase B gives insight into the enzymatic properties of a trypanosomatid virulence factor
    • McLuskey, K., Paterson, N. G., Bland, N. D., Isaacs, N. W., and Mottram, J. C. (2010) Crystal stucture of Leishmania major oligopeptidase B gives insight into the enzymatic properties of a trypanosomatid virulence factor. J. Biol. Chem. 285, 39249-39259
    • (2010) J. Biol. Chem. , vol.285 , pp. 39249-39259
    • McLuskey, K.1    Paterson, N.G.2    Bland, N.D.3    Isaacs, N.W.4    Mottram, J.C.5
  • 41
    • 43049096077 scopus 로고    scopus 로고
    • Structural and kinetic contributions of the oxyanion binding site to the catalytic activity of acylaminoacyl peptidase
    • Kiss, A. L., Palló, A., Náray-Szabó, G., Harmat, V., and Polgár, L. (2008) Structural and kinetic contributions of the oxyanion binding site to the catalytic activity of acylaminoacyl peptidase. J. Struct. Biol. 162, 312-323
    • (2008) J. Struct. Biol. , vol.162 , pp. 312-323
    • Kiss, A.L.1    Palló, A.2    Náray-Szabó, G.3    Harmat, V.4    Polgár, L.5
  • 42
    • 23044435795 scopus 로고    scopus 로고
    • Flexibility of prolyl oligopeptidase: Molecular dynamics and molecular framework analysis of the potential substrate pathways
    • DOI 10.1002/prot.20508
    • Fuxreiter, M., Magyar, C., Juhász, T., Szeltner, Z., Polgár, L., and Simon, I. (2005) Flexibility of prolyl oligopeptidase. Molecular dynamics and molecular framework analysis of the potential substrate pathways. Proteins 60, 504-512 (Pubitemid 41061642)
    • (2005) Proteins: Structure, Function and Genetics , vol.60 , Issue.3 , pp. 504-512
    • Fuxreiter, M.1    Magyar, C.2    Juhasz, T.3    Szeltner, Z.4    Polgar, L.5    Simon, I.6
  • 43
    • 0037107371 scopus 로고    scopus 로고
    • Structures of the tricorn-interacting aminopeptidase F1 with different ligands explain its catalytic mechanism
    • DOI 10.1093/emboj/cdf552
    • Goettig, P., Groll, M., Kim, J. S., Huber, R., and Brandstetter, H. (2002) Structures of the tricorn-interacting aminopeptidase F1 with different ligands explain its catalytic mechanism. EMBO J. 21, 5343-5352 (Pubitemid 35231014)
    • (2002) EMBO Journal , vol.21 , Issue.20 , pp. 5343-5352
    • Goettig, P.1    Groll, M.2    Kim, J.-S.3    Huber, R.4    Brandstetter, H.5
  • 46
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C. M. (2003) Protein folding and misfolding. Nature 426, 884-890
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 47
    • 14144256476 scopus 로고    scopus 로고
    • Protein aggregation determinants from a simplified model. Cooperative folders resist aggregation
    • Clark, L. A. (2005) Protein aggregation determinants from a simplified model. Cooperative folders resist aggregation. Protein Sci. 14, 653-662
    • (2005) Protein Sci. , vol.14 , pp. 653-662
    • Clark, L.A.1
  • 48
    • 34547631623 scopus 로고    scopus 로고
    • Prevention of amyloid-like aggregation as a driving force of protein evolution
    • DOI 10.1038/sj.embor.7401034, PII 7401034
    • Monsellier, E., and Chiti, F. (2007) Prevention of amyloid-like aggregation as a driving force of protein evolution. EMBO Rep. 8, 737-742 (Pubitemid 47202452)
    • (2007) EMBO Reports , vol.8 , Issue.8 , pp. 737-742
    • Monsellier, E.1    Chiti, F.2
  • 49
    • 28444464509 scopus 로고    scopus 로고
    • Amyloid formation of a protein in the absence of initial unfolding and destabilization of the native state
    • DOI 10.1529/biophysj.105.067538
    • Soldi, G., Bemporad, F., Torrassa, S., Relini, A., Ramazzotti, M., Taddei, N., and Chiti, F. (2005) Amyloid formation of a protein in the absence of initial unfolding and destabilization of the native state. Biophys. J. 89, 4234-4244 (Pubitemid 41725642)
    • (2005) Biophysical Journal , vol.89 , Issue.6 , pp. 4234-4244
    • Soldi, G.1    Bemporad, F.2    Torrassa, S.3    Relini, A.4    Ramazzotti, M.5    Taddei, N.6    Chiti, F.7
  • 50
    • 57749098600 scopus 로고    scopus 로고
    • Amyloid formation by globular proteins under native conditions
    • Chiti, F., and Dobson, C. M. (2009) Amyloid formation by globular proteins under native conditions. Nat. Chem. Biol. 5, 15-22
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 15-22
    • Chiti, F.1    Dobson, C.M.2
  • 51
    • 10644225416 scopus 로고    scopus 로고
    • Protein misfolding and aggregation. New examples in medicine and biology of the dark side of the protein world
    • Stefani M., (2004) Protein misfolding and aggregation. New examples in medicine and biology of the dark side of the protein world. Biochim. Biophys. Acta 1739, 5-25
    • (2004) Biochim. Biophys. Acta , vol.1739 , pp. 5-25
    • Stefani, M.1
  • 52
    • 35449003305 scopus 로고    scopus 로고
    • Truncated prolyl oligopeptidase from Pyrococcus furiosus
    • Juhász, T., Szeltner, Z., and Polgár, L. (2007) Truncated prolyl oligopeptidase from Pyrococcus furiosus. Proteins 69, 633-643
    • (2007) Proteins , vol.69 , pp. 633-643
    • Juhász, T.1    Szeltner, Z.2    Polgár, L.3
  • 53
    • 53149110079 scopus 로고    scopus 로고
    • The conserved N-terminal helix of acylpeptide hydrolase from archaeon Aeropyrum pernix K1 is important for its hyperthermophilic activity
    • Zhang, Z., Zheng, B., Wang, Y., Chen, Y., Manco, G., and Feng, Y. (2008) The conserved N-terminal helix of acylpeptide hydrolase from archaeon Aeropyrum pernix K1 is important for its hyperthermophilic activity. Biochim. Biophys. Acta 1784, 1176-1183
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 1176-1183
    • Zhang, Z.1    Zheng, B.2    Wang, Y.3    Chen, Y.4    Manco, G.5    Feng, Y.6
  • 54
    • 0025734772 scopus 로고
    • Crystal structure of haloalkane dehalogenase: An enzyme to detoxify halogenated alkanes
    • Franken, S. M., Rozeboom, H. J., Kalk, K. H., and Dijkstra, B. W. (1991) Crystal structure of haloalkane dehalogenase. An enzyme to detoxify halogenated alkanes. EMBO J. 10, 1297-1302 (Pubitemid 21905592)
    • (1991) EMBO Journal , vol.10 , Issue.6 , pp. 1297-1302
    • Franken, S.M.1    Rozeboom, H.J.2    Kalk, K.H.3    Dijkstra, B.W.4
  • 55
    • 0025160881 scopus 로고
    • Refined structure of dienelactone hydrolase at 1.8 Å
    • DOI 10.1016/0022-2836(90)90196-S
    • Pathak, D., and Ollis, D. (1990) Refined structure of dienelactone hydrolase at 1.8 Å. J. Mol. Biol. 214, 497-525 (Pubitemid 20261980)
    • (1990) Journal of Molecular Biology , vol.214 , Issue.2 , pp. 497-525
    • Pathak, D.1    Ollis, D.2
  • 59
    • 48449095141 scopus 로고    scopus 로고
    • The molecular structure of epoxide hydrolase B from Mycobacterium tuberculosis and its complex with a urea-based inhibitor
    • Biswal, B. K., Morisseau, C., Garen, G., Cherney, M. M., Garen, C., Niu, C., Hammock, B. D., and James, M. N. (2008) The molecular structure of epoxide hydrolase B from Mycobacterium tuberculosis and its complex with a urea-based inhibitor. J. Mol. Biol. 381, 897-912
    • (2008) J. Mol. Biol. , vol.381 , pp. 897-912
    • Biswal, B.K.1    Morisseau, C.2    Garen, G.3    Cherney, M.M.4    Garen, C.5    Niu, C.6    Hammock, B.D.7    James, M.N.8
  • 60
    • 52049088539 scopus 로고    scopus 로고
    • Atomic resolution crystal structures and quantum chemistry meet to reveal subtleties of hydroxynitrile lyase catalysis
    • Schmidt, A., Gruber, K., Kratky, C., and Lamzin, V. S. (2008) Atomic resolution crystal structures and quantum chemistry meet to reveal subtleties of hydroxynitrile lyase catalysis. J. Biol. Chem. 283, 21827-21836
    • (2008) J. Biol. Chem. , vol.283 , pp. 21827-21836
    • Schmidt, A.1    Gruber, K.2    Kratky, C.3    Lamzin, V.S.4
  • 61
    • 33947378334 scopus 로고    scopus 로고
    • Weak activity of haloalkane dehalogenase LinB with 1,2,3-trichloropropane revealed by X-ray crystallography and microcalorimetry
    • DOI 10.1128/AEM.02416-06
    • Monincová, M., Prokop, Z., Vévodová, J., Nagata, Y., and Damborsky, J. (2007) Weak activity of haloalkane dehalogenase LinB with 1,2,3-trichloropropane revealed by x-ray crystallography and microcalorimetry. Appl. Environ. Microbiol. 73, 2005-2008 (Pubitemid 46449086)
    • (2007) Applied and Environmental Microbiology , vol.73 , Issue.6 , pp. 2005-2008
    • Monincova, M.1    Prokop, Z.2    Vevodova, J.3    Nagata, Y.4    Damborsky, J.5
  • 62
    • 79960922176 scopus 로고    scopus 로고
    • The unusual extended C-terminal helix of the peroxisomal α/β-hydrolase Lpx1 is involved in dimer contacts but dispensable for dimerization
    • Thoms, S., Hofhuis, J., Thöing, C., Gärtner, J., and Niemann, H. H. (2011) The unusual extended C-terminal helix of the peroxisomal α/β-hydrolase Lpx1 is involved in dimer contacts but dispensable for dimerization. J. Struct. Biol. 175, 362-371
    • (2011) J. Struct. Biol. , vol.175 , pp. 362-371
    • Thoms, S.1    Hofhuis, J.2    Thöing, C.3    Gärtner, J.4    Niemann, H.H.5
  • 63
    • 0025744320 scopus 로고
    • Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase
    • Rould M. A., Perona J. J., and Steitz T. A. (1991) Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase. Nature 352, 213-218 (Pubitemid 21912313)
    • (1991) Nature , vol.352 , Issue.6332 , pp. 213-218
    • Rould, M.A.1    Perona, J.J.2    Steitz, T.A.3
  • 64
    • 0032472380 scopus 로고    scopus 로고
    • Structure of proline iminopeptidase from Xanthomonas campestris pv. citri: A prototype for the prolyl oligopeptidase family
    • DOI 10.1093/emboj/17.1.1
    • Medrano, F. J., Alonso, J., García, J. L., Romero, A., Bode, W., and Gomis- Rüth, F. X. (1998) Structure of proline iminopeptidase from Xanthomonas campestris pv. citri. A prototype for the prolyl oligopeptidase family. EMBO J. 17, 1-9 (Pubitemid 28041043)
    • (1998) EMBO Journal , vol.17 , Issue.1 , pp. 1-9
    • Medrano, F.J.1    Alonso, J.2    Garcia, J.L.3    Romero, A.4    Bode, W.5    Gomis-Ruth, F.X.6


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