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PDBsum entry 1mey
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Transferase/DNA
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PDB id
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1mey
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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A 2.2 a resolution crystal structure of a designed zinc finger protein bound to DNA.
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Authors
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C.A.Kim,
J.M.Berg.
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Ref.
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Nat Struct Biol, 1996,
3,
940-945.
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PubMed id
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Abstract
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Considerable recent effort has been devoted to the design and selection of
sequence-specific DNA binding proteins based on tandem arrays of Cys2His2 zinc
finger domains. While the DNA binding properties of these designed proteins have
been studied extensively, the structural basis for site-specific binding has not
been examined experimentally. Here we report the crystal structure of a complex
between a protein comprised of three consensus-sequence-based zinc finger
domains and an oligonucleotide corresponding to a favourable DNA binding site.
This structure reveals relatively simple modular interactions and structural
adaptations that compensate for differences in contact residue side-chain
lengths.
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Secondary reference #1
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Title
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Serine at position 2 in the DNA recognition helix of a cys2-His2 zinc finger peptide is not, In general, Responsible for base recognition.
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Authors
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C.A.Kim,
J.M.Berg.
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Ref.
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J Mol Biol, 1995,
252,
1-5.
[DOI no: ]
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PubMed id
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Figure 1.
Figure 1. The sequences of the zinc finger proteins used
in this study. Each of the last three lines represents an
individual zinc finger domain. The amino acid residues in
bold indicate positions - 1, 3 and 6 of the recognition helix.
The variants constructed for this study differed at the
positions marked with an X in finger two. The genes
encoding the various peptides were constructed and the
peptides expressed and partially purified as previously
described (Desjarlais & Berg, 1992a,b, 1993). A bacterio-
phage T7-based vector (Studier et al., 1990) expression
system was used in this study.
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Figure 3.
Figure 3. A side-by-side compari-
son of the selection results for the
HSSNLQK, ASSNLQK, and HSAN-
LQK proteins. The similarity in
these profiles suggests that histidine
in position -1 does not contribute
extensively to DNA binding site
determination nor is the identity of
the residue in position 2 (serine or
alanine) important.
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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Secondary reference #2
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Title
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Crystal structure of a five-Finger gli-Dna complex: new perspectives on zinc fingers.
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Authors
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N.P.Pavletich,
C.O.Pabo.
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Ref.
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Science, 1993,
261,
1701-1707.
[DOI no: ]
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PubMed id
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Secondary reference #3
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Title
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The crystal structure of a two zinc-Finger peptide reveals an extension to the rules for zinc-Finger/DNA recognition.
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Authors
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L.Fairall,
J.W.Schwabe,
L.Chapman,
J.T.Finch,
D.Rhodes.
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Ref.
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Nature, 1993,
366,
483-487.
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PubMed id
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Secondary reference #4
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Title
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Zinc finger-Dna recognition: crystal structure of a zif268-Dna complex at 2.1 a.
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Authors
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N.P.Pavletich,
C.O.Pabo.
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Ref.
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Science, 1991,
252,
809-817.
[DOI no: ]
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PubMed id
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