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Volumn 62, Issue 2, 2006, Pages 555-556

Crystal structure of ADP/AMP complex of Escherichia coli adenylate kinase

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; ADENYLATE KINASE; BACTERIAL ENZYME;

EID: 30144436102     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20699     Document Type: Article
Times cited : (35)

References (9)
  • 1
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    • Movie of the structural changes during a catalytic cycle of nucleoside monophosphate kinases
    • Vonrhein C, Schlauderer G, Schulz GE. Movie of the structural changes during a catalytic cycle of nucleoside monophosphate kinases. Structure 1995;3:483-490.
    • (1995) Structure , vol.3 , pp. 483-490
    • Vonrhein, C.1    Schlauderer, G.2    Schulz, G.E.3
  • 2
    • 0025302757 scopus 로고
    • Mechanism of adenylate kinase. Structural and functional demonstration of arginine-138 as a key catalytic residue that cannot be replaced by lysine
    • Yan H, Shi Z, Tsai M-D. Mechanism of adenylate kinase. Structural and functional demonstration of arginine-138 as a key catalytic residue that cannot be replaced by lysine. Biochemistry 1990;29:6385-6392.
    • (1990) Biochemistry , vol.29 , pp. 6385-6392
    • Yan, H.1    Shi, Z.2    Tsai, M.-D.3
  • 4
    • 0028338283 scopus 로고
    • The closed conformation of a highly flexible protein: The structure of E. coli adenylate kinase with bound AMP and AMPPNP
    • Berry MB, Meador B, Bilderback T, Liang P, Glaser M, Phillips GN Jr. The closed conformation of a highly flexible protein: the structure of E. coli adenylate kinase with bound AMP and AMPPNP. Proteins 1994;19:183-198.
    • (1994) Proteins , vol.19 , pp. 183-198
    • Berry, M.B.1    Meador, B.2    Bilderback, T.3    Liang, P.4    Glaser, M.5    Phillips Jr., G.N.6
  • 5
    • 0029871765 scopus 로고    scopus 로고
    • Substrate binding causes movement in the ATP binding domain of Escherichia coli adenylate kinase
    • Bilderback T, Fulmer T, Mantulin WW, Glaser M. Substrate binding causes movement in the ATP binding domain of Escherichia coli adenylate kinase. Biochemistry 1996;35:6100-6106.
    • (1996) Biochemistry , vol.35 , pp. 6100-6106
    • Bilderback, T.1    Fulmer, T.2    Mantulin, W.W.3    Glaser, M.4
  • 6
    • 0003769049 scopus 로고
    • New Haven, CT: The Howard Hughes Medical Institute and Department of Molecular Biophysics and Biochemistry, Yale University
    • Brünger AT. X-PLOR, Version 3.1, A system for X-ray crystallography and NMR. New Haven, CT: The Howard Hughes Medical Institute and Department of Molecular Biophysics and Biochemistry, Yale University; 1992.
    • (1992) X-PLOR, Version 3.1, a System for X-Ray Crystallography and NMR
    • Brünger, A.T.1
  • 7
    • 0029866802 scopus 로고    scopus 로고
    • Structure of a mutant adenylate kinase ligated with an ATP-analogue showing domain closure over ATP
    • Schlauderer GJ, Proba K, Schulz GE. Structure of a mutant adenylate kinase ligated with an ATP-analogue showing domain closure over ATP. J Mol Biol 1996;256:223-227.
    • (1996) J Mol Biol , vol.256 , pp. 223-227
    • Schlauderer, G.J.1    Proba, K.2    Schulz, G.E.3
  • 8
    • 0014429881 scopus 로고
    • Initial velocity and equilibrium kinetics of myokinase
    • Rhoads DG, Lowenstein JM. Initial velocity and equilibrium kinetics of myokinase. J Biol Chem 1968;243:3963-3972.
    • (1968) J Biol Chem , vol.243 , pp. 3963-3972
    • Rhoads, D.G.1    Lowenstein, J.M.2
  • 9
    • 0038690122 scopus 로고    scopus 로고
    • Structures of thermophilic and mesophilic adenylate kinases from the genus Methanococcus
    • Criswell AR, Bae E, Stec B, Konisky J, Phillips GN Jr. Structures of thermophilic and mesophilic adenylate kinases from the genus Methanococcus. J Mol Biol 2003;330:1087-1099.
    • (2003) J Mol Biol , vol.330 , pp. 1087-1099
    • Criswell, A.R.1    Bae, E.2    Stec, B.3    Konisky, J.4    Phillips Jr., G.N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.