Related ArticlesAlternating zinc fingers in the human male associated protein ZFY: 2D NMR structure of an even finger and implications for "jumping-linker" DNA recognition.
Biochemistry. 1991 Apr 9;30(14):3371-86
Authors: Kochoyan M, Havel TF, Nguyen DT, Dahl CE, Keutmann HT, Weiss MA
ZFY, a sex-related Zn-finger protein encoded by the human Y chromosome, is distinguished from the general class of Zn-finger proteins by the presence of a two-finger repeat. Whereas odd-numbered domains and linkers fit a general consensus, even-numbered domains and linkers exhibit systematic differences. Because this alternation may have fundamental implications for the mechanism of protein-DNA recognition, we have undertaken biochemical and structural studies of fragments of ZFY. We describe here the solution structure of a representative nonconsensus (even-numbered) Zn finger based on 2D NMR studies of a 30-residue peptide. Structural modeling by distance geometry and simulated annealing (DG/SA) demonstrates that this peptide folds as a miniglobular domain containing a C-terminal beta--hairpin and N-terminal alpha-helix (beta beta alpha motif). These features are similar to (but not identical with) those previously described in consensus-type Zn fingers (derived from ADR1 and Xfin); the similarities suggest that even and odd ZFY domains bind DNA by a common mechanism. A model of the protein-DNA complex (designated the "jumping-linker" model) is presented and discussed in terms of the ZFY two-finger repeat. In this model every other linker is proposed to cross the minor groove by means of a putative finger/linker submotif HX4HX3-hydrophobic residue-X3. Analogous use of a hydrophobic residue in a linker that spans the minor groove has recently been described in crystallographic and 3D NMR studies of homeodomain-DNA complexes. The proposed model of ZFY is supported in part by the hydroxyl radical footprint of the TFIIIA-DNA complex [Churchill, M.E.A., Tullius, T.D., & Klug, A. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 5528-5532].
[NMR paper] Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc
Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc bound at the active site.
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J Mol Biol. 2004 Nov 19;344(2):567-83
Authors: Ramelot TA, Cort JR, Goldsmith-Fischman S, Kornhaber GJ, Xiao R, Shastry R, Acton TB, Honig B, Montelione GT, Kennedy MA
IscU is a highly conserved protein that serves as the scaffold for IscS-mediated assembly of iron-sulfur () clusters. We report the NMR...
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[NMR paper] NMR structure of the complex between the zinc finger protein NCp10 of Moloney murine
NMR structure of the complex between the zinc finger protein NCp10 of Moloney murine leukemia virus and the single-stranded pentanucleotide d(ACGCC): comparison with HIV-NCp7 complexes.
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Biochemistry. 1999 Oct 5;38(40):12984-94
Authors: Schüler W, Dong C, Wecker K, Roques BP
The structure of the 56 amino acid nucleocapsid protein NCp10 of...
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[NMR paper] Secondary structure and zinc ligation of human recombinant short-form stromelysin by
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Biochemistry. 1993 Dec 7;32(48):13098-108
Authors: Gooley PR, Johnson BA, Marcy AI, Cuca GC, Salowe SP, Hagmann WK, Esser CK, Springer JP
Stromelysin-1, a member of the matrix metalloendoprotease family, is a zinc protease involved in the degradation of connective tissue in the...
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[NMR paper] Zinc- and sequence-dependent binding to nucleic acids by the N-terminal zinc finger o
Zinc- and sequence-dependent binding to nucleic acids by the N-terminal zinc finger of the HIV-1 nucleocapsid protein: NMR structure of the complex with the Psi-site analog, dACGCC.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Zinc- and sequence-dependent binding to nucleic acids by the N-terminal zinc finger of the HIV-1 nucleocapsid protein: NMR...
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[NMR paper] Binding of cadmium(II) and zinc(II) to human and dog serum albumins. An equilibrium d
Binding of cadmium(II) and zinc(II) to human and dog serum albumins. An equilibrium dialysis and 113Cd-NMR study.
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Biochem Cell Biol. 1991 Dec;69(12):809-20
Authors: Goumakos W, Laussac JP, Sarkar B
The binding of Cd(II) and Zn(II) to human serum albumin (HSA) and dog serum albumin (DSA) has been studied by equilibrium dialysis and 113Cd(II)-NMR techniques at physiological pH. Scatchard analysis of the equilibrium...
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[NMR paper] Binding of cadmium(II) and zinc(II) to human and dog serum albumins. An equilibrium d
Binding of cadmium(II) and zinc(II) to human and dog serum albumins. An equilibrium dialysis and 113Cd-NMR study.
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Biochem Cell Biol. 1991 Dec;69(12):809-20
Authors: Goumakos W, Laussac JP, Sarkar B
The binding of Cd(II) and Zn(II) to human serum albumin (HSA) and dog serum albumin (DSA) has been studied by equilibrium dialysis and 113Cd(II)-NMR techniques at physiological pH. Scatchard analysis of the equilibrium...
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[NMR paper] Alternating zinc fingers in the human male associated protein ZFY: refinement of the
Alternating zinc fingers in the human male associated protein ZFY: refinement of the NMR structure of an even finger by selective deuterium labeling and implications for DNA recognition.
Alternating zinc fingers in the human male associated protein ZFY: refinement of the NMR structure of an even finger by selective deuterium labeling and implications for DNA recognition.
Biochemistry. 1991 Jul 23;30(29):7063-72
Authors: Kochoyan M, Keutmann HT, Weiss MA
ZFY, a male-associated Zn-finger protein encoded by the human Y chromosome, exhibits a...
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[NMR paper] Alternating zinc fingers in the human male associated protein ZFY: refinement of the
Alternating zinc fingers in the human male associated protein ZFY: refinement of the NMR structure of an even finger by selective deuterium labeling and implications for DNA recognition.
Alternating zinc fingers in the human male associated protein ZFY: refinement of the NMR structure of an even finger by selective deuterium labeling and implications for DNA recognition.
Biochemistry. 1991 Jul 23;30(29):7063-72
Authors: Kochoyan M, Keutmann HT, Weiss MA
ZFY, a male-associated Zn-finger protein encoded by the human Y chromosome, exhibits a...
Alternating zinc fingers in the human male associated protein ZFY: 2D NMR structure o
Linear Mode
