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Volumn 1435, Issue 1-2, 1999, Pages 7-21

Crystal structure at 1.63 Å resolution of the native form of porcine β-trypsin: Revealing an acetate ion binding site and functional water network

Author keywords

Acetate ion binding; Calcium ion binding; Functional water; Orientation of the catalytic triad; Porcine trypsin

Indexed keywords

ACETIC ACID; ASPARTIC ACID; HISTIDINE; PROTEINASE INHIBITOR; SERINE; SERINE PROTEINASE; SULFATE; TRYPSIN; WATER;

EID: 0032724963     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(99)00202-2     Document Type: Article
Times cited : (16)

References (30)
  • 2
  • 3
    • 0016796849 scopus 로고
    • The refined crystal structure of bovine beta trypsin at 1.8 Å resolution. II Crystallographic refinement, calcium binding site, benzamidine binding site and active site at pH 7.0
    • Bode W., Schwager P. The refined crystal structure of bovine beta trypsin at 1.8 Å resolution. II Crystallographic refinement, calcium binding site, benzamidine binding site and active site at pH 7.0. J. Mol. Biol. 98:1975;693-717.
    • (1975) J. Mol. Biol. , vol.98 , pp. 693-717
    • Bode, W.1    Schwager, P.2
  • 4
    • 0030954450 scopus 로고    scopus 로고
    • The first crystal structure at 1.8 Å resolution of an active autolysate form of porcine α trypsin
    • Johnson A., Krishnaswamy S., Sundram P.V., Pattabhi V. The first crystal structure at 1.8 Å resolution of an active autolysate form of porcine α trypsin. Acta. Cryst. D53:1997;311-315.
    • (1997) Acta. Cryst. , vol.53 , pp. 311-315
    • Johnson, A.1    Krishnaswamy, S.2    Sundram, P.V.3    Pattabhi, V.4
  • 5
    • 0027941821 scopus 로고
    • Refined 1.8 Å resolution crystal structure of the porcine ε trypsin
    • Huang Q., Wang Z., Li Y., Liu S., Tang Y. Refined 1.8 Å resolution crystal structure of the porcine ε trypsin. Biochem. Biophys. Acta. 1209:1994;77-82.
    • (1994) Biochem. Biophys. Acta , vol.1209 , pp. 77-82
    • Huang, Q.1    Wang, Z.2    Li, Y.3    Liu, S.4    Tang, Y.5
  • 6
    • 0027516857 scopus 로고
    • Refined 1.6 Å resolution crystal structure of the complex formed between porcine β-trypsin and MCTI-A, a trypsin inhibitor of the squash family. Detailed comaprsion with the bovine β trypsin and its complxes
    • Huang Q., Liu S., Tang Y. Refined 1.6 Å resolution crystal structure of the complex formed between porcine β-trypsin and MCTI-A, a trypsin inhibitor of the squash family. Detailed comaprsion with the bovine β trypsin and its complxes. J. Mol. Biol. 229:1993;1022-1036.
    • (1993) J. Mol. Biol. , vol.229 , pp. 1022-1036
    • Huang, Q.1    Liu, S.2    Tang, Y.3
  • 7
    • 0024791521 scopus 로고
    • Crystal structure of bovine β-trypsin at 1.5 Å resolution in a crystal form with low molecular packing density
    • Bartunik H.D., Summess L.J., Bartsh H.H. Crystal structure of bovine β-trypsin at 1.5 Å resolution in a crystal form with low molecular packing density. J. Mol. Biol. 210:1989;813-828.
    • (1989) J. Mol. Biol. , vol.210 , pp. 813-828
    • Bartunik, H.D.1    Summess, L.J.2    Bartsh, H.H.3
  • 8
    • 84977303841 scopus 로고
    • The geometry of the reactive site and of the peptide groups in Trypsin. Trypsinogen and its complexes with inhibitors
    • Marquart M., Walter J., Deisenhofer J., Bode W., Huber R. The geometry of the reactive site and of the peptide groups in Trypsin. Trypsinogen and its complexes with inhibitors. Acta Cryst. B39:1983;480-490.
    • (1983) Acta Cryst. , vol.39 , pp. 480-490
    • Marquart, M.1    Walter, J.2    Deisenhofer, J.3    Bode, W.4    Huber, R.5
  • 9
    • 0019334147 scopus 로고
    • Neutron diffraction identifies His 57 as the catalytic base in trypsin
    • Kossiakoff A.A., Spencer S.A. Neutron diffraction identifies His 57 as the catalytic base in trypsin. Nature (Lond.). 288:1980;414-416.
    • (1980) Nature (Lond.) , vol.288 , pp. 414-416
    • Kossiakoff, A.A.1    Spencer, S.A.2
  • 11
    • 0001650759 scopus 로고
    • Theoretical correlation of structure and energetics in the catalytic reaction of trypsin
    • Warshel A., Russell S. Theoretical correlation of structure and energetics in the catalytic reaction of trypsin. J. Am. Chem. Soc. 108:1986;6569-6579.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 6569-6579
    • Warshel, A.1    Russell, S.2
  • 12
    • 0014689979 scopus 로고
    • Role of buried acid group in the mechanism of action of chymotrypsin
    • Blow D.M., Birkcoft J., Hartley B.S. Role of buried acid group in the mechanism of action of chymotrypsin. Nature (Lond.). 221:1969;337-340.
    • (1969) Nature (Lond.) , vol.221 , pp. 337-340
    • Blow, D.M.1    Birkcoft, J.2    Hartley, B.S.3
  • 13
    • 50549163362 scopus 로고
    • The preparation and properties of two new chromogenic substrates of trypsin
    • Erlanger K.E., Kokowsky N., Cohen W. The preparation and properties of two new chromogenic substrates of trypsin. Arch. Biochem. Biophys. 95:1961;271-278.
    • (1961) Arch. Biochem. Biophys. , vol.95 , pp. 271-278
    • Erlanger, K.E.1    Kokowsky, N.2    Cohen, W.3
  • 15
    • 0002660809 scopus 로고
    • The detection of sub-units within the Crystallographic asymmetric unit
    • Rossmann M.G., Ilow D.M. The detection of sub-units within the Crystallographic asymmetric unit. Acta Cryst. 15:1962;24-31.
    • (1962) Acta Cryst. , vol.15 , pp. 24-31
    • Rossmann, M.G.1    Ilow, D.M.2
  • 16
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brunger A.T., Kuriyen J., Karplus M. Crystallographic R factor refinement by molecular dynamics. Science. 235:1987;458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brunger, A.T.1    Kuriyen, J.2    Karplus, M.3
  • 17
    • 84901961522 scopus 로고
    • Slow- cooling protocols for Crystallographic refinement by simulated annealing
    • Brunger A.T., Kurkawski A. Slow- cooling protocols for Crystallographic refinement by simulated annealing. Acta Cryst. A46:1990;585-593.
    • (1990) Acta Cryst. , vol.46 , pp. 585-593
    • Brunger, A.T.1    Kurkawski, A.2
  • 19
    • 0028103275 scopus 로고
    • Collaborative Computational Project, Number 4, The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4, The CCP4 suite: programs for protein crystallography, Acta Cryst. D50, 1994, pp. 760-763.
    • (1994) Acta Cryst. , vol.D50 , pp. 760-763
  • 20
    • 0344736073 scopus 로고
    • Biosym, San Diego, CA
    • Biosym, Insight II. Biosym, San Diego, CA, 1993.
    • (1993) Biosym, Insight II.
  • 21
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometric features
    • Kabsch W., Sandor C. Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometric features. Bioploymers. 22:1983;2577-2637.
    • (1983) Bioploymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sandor, C.2
  • 23
    • 0000243829 scopus 로고
    • PROCHECK: Aprogram to check the stereochemical quality of protein structures
    • Laskowski R.A., MacArthur M.W., Moss D.S., Thronton J.M. PROCHECK: aprogram to check the stereochemical quality of protein structures. J. Appl. Cryst. 26:1993;283-291.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thronton, J.M.4
  • 24
    • 33947092515 scopus 로고
    • Structural basis of the activation and action of trypsin
    • Huber R., Bode W. Structural basis of the activation and action of trypsin. Acc. Chem. Res. 11:1978;119-122.
    • (1978) Acc. Chem. Res. , vol.11 , pp. 119-122
    • Huber, R.1    Bode, W.2
  • 26
    • 0014477895 scopus 로고
    • Studiesof the conformation and interaction in dinucleoside mono- And diphosphates by proton magnetic resonance
    • Ts'o P.O.P., Kondo N.S., Schweizer M.P., Hollis D.P. Studiesof the conformation and interaction in dinucleoside mono- and diphosphates by proton magnetic resonance. Biochemistry. 8:1969;997-1029.
    • (1969) Biochemistry , vol.8 , pp. 997-1029
    • Ts'O, P.O.P.1    Kondo, N.S.2    Schweizer, M.P.3    Hollis, D.P.4
  • 27
    • 0024290411 scopus 로고    scopus 로고
    • A solution structure for poly(rA).poly(dT) with different furanose pucker and backbone geometry in rA and dT strands and intrastrand hydrogen bonding of adenine 8CH
    • Benevides J.M., Thomas G.J. A solution structure for poly(rA).poly(dT) with different furanose pucker and backbone geometry in rA and dT strands and intrastrand hydrogen bonding of adenine 8CH. Biochemistry. 27:1998;3868-3873.
    • (1998) Biochemistry , vol.27 , pp. 3868-3873
    • Benevides, J.M.1    Thomas, G.J.2
  • 29
    • 0014670506 scopus 로고
    • Pseudotrypsin, amodified bovine trypsin produced by limited autodigestion
    • Smith R.L., Shaw E. Pseudotrypsin, amodified bovine trypsin produced by limited autodigestion. J. Mol. Chem. 244:1969;4704-4707.
    • (1969) J. Mol. Chem. , vol.244 , pp. 4704-4707
    • Smith, R.L.1    Shaw, E.2
  • 30
    • 0001099937 scopus 로고
    • Traitement statitique des erreurs dans la determination des structures cristallines
    • Luzzati V. Traitement statitique des erreurs dans la determination des structures cristallines. Acta Cryst. 5:1952;802-810.
    • (1952) Acta Cryst. , vol.5 , pp. 802-810
    • Luzzati, V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.