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Volumn 43, Issue 5, 2004, Pages 1708-1713

Hydrolytic Reaction by Zinc Finger Mutant Peptides: Successful Redesign of Structural Zinc Sites into Catalytic Zinc Sites

Author keywords

[No Author keywords available]

Indexed keywords

4 NITROPHENYL ACETATE; ACETIC ACID DERIVATIVE; AMINO ACID; CYSTEINYLCYSTEINYLHISTIDYLGLYCINE; CYSTEINYLCYSTEINYLHISTIDYLHISTIDINE; ESTER; FUNCTIONAL GROUP; GLYCYLCYSTEINYLHISTIDYLHISTIDINE; HYDROXIDE; MUTANT PROTEIN; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG; WATER; ZINC; ZINC COMPLEX; ZINC FINGER PROTEIN; ZINC ION;

EID: 1542317534     PISSN: 00201669     EISSN: None     Source Type: Journal    
DOI: 10.1021/ic034931y     Document Type: Article
Times cited : (48)

References (52)
  • 7
    • 0035690880 scopus 로고    scopus 로고
    • Auld, D. S. BioMetals 2001, 14, 271-313.
    • (2001) BioMetals , vol.14 , pp. 271-313
    • Auld, D.S.1
  • 10
    • 0025994794 scopus 로고
    • Klevit, R. E. Science 1991, 253, 1367-1393.
    • (1991) Science , vol.253 , pp. 1367-1393
    • Klevit, R.E.1
  • 31
    • 1542309628 scopus 로고    scopus 로고
    • note
    • -8) for the Zn(II)-peptide complexes.27
  • 35
    • 1542309632 scopus 로고    scopus 로고
    • note
    • Although the NMR chemical shifts and NOEs of the histidine imidazole groups suggest three or four histidine imidazole residues in contact with Zn(II), the NMR data provided little information about the Zn(II) coordination geometry. The NMR structure34 was calculated on the basis of the assumption that the zinc was tetrahedrally coordinated as can be seen in the wild type.49 The visible spectra of the corresponding Co(II) complex and the high catalytic activity of the Zn(II) complex strongly suggest a 6-coordination rather than a 4-coordination for the mutant complex Zn(II)-zf(HHHH). In contrast, the wild complex Zn(II)-zf(CCHH) exactly adopts a tetrahedral geometry through two cysteine and two histidene residues, consistent with the spectral data of the Co(II) complex and no catalytic activity of the Zn(II) complex.
  • 37
    • 1542369373 scopus 로고    scopus 로고
    • note
    • The d-d bands of Co(II)-zf(HHHH) and the pH dependence of the hydrolytic activity suggest that the zinc center of Zn(II)-zf(HHHH) should adopt a six-coordinate geometry rather than a tetrahedral geometry (Figures 5 and S1), although we have assumed in the previous report that each zinc finger motif of the related three tandem Zn(II)-zf(HHHH) protein has a tetrahedral geometry.34 The three tandem Zn(II)-zf(HHHH) proteins have a high affinity for DNA, despite the structural change of the zinc site from a tetrahedral to a six-coordinate geometry. The three tandem Zn(II)-zf(HHHH) proteins exhibit an α-helix induction upon Zn(II) binding, whose helicity is comparable to the wild type. (The present Zn(II)-zf(HHHH) peptide also induces an α-helix to a similar extent as the wild type.) As well-known, the α-helix region of zinc finger motifs plays a central role in DNA recognition. We think that is the reason the Zn(II)-zf(HHHH) protein retains a high affinity for DNA. The structural change of the zinc center might not significantly decrease the DNA affinity for Zn(II)-zf(HHHH).
  • 47
    • 1542309630 scopus 로고    scopus 로고
    • note
    • m value.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.