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Volumn 306, Issue 4, 2001, Pages 851-861

Catalytic efficiency and sequence selectivity of a restriction endonuclease modulated by a distal manganese ion binding site

Author keywords

Indirect readout; Metal ion catalysis; Protein engineering; Protein nucleic acid recognition

Indexed keywords

CALCIUM ION; DNA; MANGANESE; RESTRICTION ENDONUCLEASE;

EID: 0035793706     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.4434     Document Type: Article
Times cited : (19)

References (50)
  • 3
    • 0026019625 scopus 로고
    • Structural basis for the 3′-5′ exonuclease activity of Escherichia coli DNA polymerase I: A two metal ion mechanism
    • (1991) EMBO J. , vol.10 , pp. 25-33
    • Beese, L.J.1    Steitz, T.A.2
  • 13
    • 0032555574 scopus 로고    scopus 로고
    • Recognition of flanking DNA sequences by EcoRV endonuclease involves alternative patterns of water-mediated contacts
    • (1998) J. Biol. Chem. , vol.273 , pp. 21721-21729
    • Horton, N.C.1    Perona, J.J.2
  • 20
    • 0029120464 scopus 로고
    • Structural-perturbation approaches to thermodynamics of site-specific protein-DNA interactions
    • (1995) Methods Enzymol. , vol.259 , pp. 305-344
    • Jen-Jacobson, L.1
  • 21
    • 0030736323 scopus 로고    scopus 로고
    • Protein-DNA recognition complexes: Conservation of structure and binding energy in the transition state
    • (1997) Biopolymers , vol.44 , pp. 153-180
    • Jen-Jacobson, L.1
  • 23
    • 0028988416 scopus 로고
    • 2+ binding to the active site of EcoRV endonuclease - A crystallographic study of complexes with substrate and product DNA at 2 Å resolution
    • (1995) Biochemistry , vol.34 , pp. 683-696
    • Kostrewa, D.1    Winkler, F.K.2
  • 26
    • 0032538280 scopus 로고    scopus 로고
    • Towards the design of rare-cutting restriction endonucleases: Using directed evolution to generate variants of EcoRV differing in their substrate specificity by two orders of magnitude
    • (1998) J. Mol. Biol. , vol.283 , pp. 59-69
    • Lanio, T.1    Jeltsch, A.2    Pingoud, A.3
  • 27
    • 0034026486 scopus 로고    scopus 로고
    • On the possibilities and limitations of rational protein design to expand the specificity of restriction enzymes: A case study employing EcoRV as the target
    • (2000) Protein Eng. , vol.13 , pp. 275-281
    • Lanio, T.1    Jeltsch, A.2    Pingoud, A.3
  • 33
    • 0031576347 scopus 로고    scopus 로고
    • Conformational transitions and structural deformability of EcoRV restriction endonuclease revealed by crystallographic analysis
    • (1997) J. Mol. Biol. , vol.273 , pp. 207-225
    • Perona, J.J.1    Martin, A.M.2
  • 36
    • 0033599296 scopus 로고    scopus 로고
    • 2+-dependent catalysis by restriction enzymes: Pre-steady state analysis of EcoRV endonuclease reveals burst kinetics and the origins of reduced activity
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 1444-1447
    • Sam, M.D.1    Perona, J.J.2
  • 41
    • 0026569359 scopus 로고
    • The activity of the EcoRV restriction endonuclease is influenced by flanking DNA sequences both inside and outside the DNA-protein complex
    • (1992) Biochemistry , vol.31 , pp. 90-97
    • Taylor, J.D.1    Halford, S.E.2
  • 49
    • 0032562147 scopus 로고    scopus 로고
    • Engineering of variants of the restriction endonuclease EcoRV that depend in their cleavage activity on the flexibility of sequences flanking the recognition site
    • (1998) Biochemistry , vol.37 , pp. 2234-2242
    • Wenz, C.1    Hahn, M.2    Pingoud, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.