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PDBsum entry 1liq
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Protein binding
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PDB id
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1liq
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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 new zinc binding fold underlines the versatility of zinc binding modules in protein evolution.
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Authors
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B.K.Sharpe,
J.M.Matthews,
A.H.Kwan,
A.Newton,
D.A.Gell,
M.Crossley,
J.P.Mackay.
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Ref.
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Structure, 2002,
10,
639-648.
[DOI no: ]
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PubMed id
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Abstract
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Many different zinc binding modules have been identified. Their abundance and
variety suggests that the formation of zinc binding folds might be relatively
common. We have determined the structure of CH1(1), a 27-residue peptide derived
from the first cysteine/histidine-rich region (CH1) of CREB binding protein
(CBP). This peptide forms a highly ordered zinc-dependent fold that is distinct
from known folds. The structure differs from a subsequently determined structure
of a larger region from the CH3 region of CBP, and the CH1(1) fold probably
represents a nonphysiologically active form. Despite this, the fold is
thermostable and tolerant to both multiple alanine mutations and changes in the
zinc-ligand spacing. Our data support the idea that zinc binding domains may
arise frequently. Additionally, such structures may prove useful as scaffolds
for protein design, given their stability and robustness.
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Figure 3.
Figure 3. Solution Structure of CH1[1](A) Stereoviews of
the best 20 structures. Structures are superimposed for best fit
over backbone atoms of residues 1-23 (note that residues 25-27
are not displayed, for clarity). Zinc-ligating side chains, red;
zinc atom, gray; side chains of well-defined residues (2, 4, 7,
9, 12, 16, 21, and 22), green.(B) Ribbon diagram of the lowest
energy structure of CH1[1]. The secondary structural elements
recognized by the program MOLMOL [33] are shown.(C) Schematic
zinc binding domain. Zinc binding domains can generally be
thought of as two bidentate zinc-ligating motifs separated by an
intervening sequence of highly variable length.(D) Overlay of
the C-X[4]-C motifs in CH1[1] and TAZ2. Residues 5-10 of CH1[1]
have been overlayed with residues 28-33 of TAZ2 (yellow) using
the backbone atoms only. The rmsd is 0.42 Å.(E) Overlay of the
H-X[3]-C motifs in CH1[1] and TAZ2. Residues 16-23 of CH1[1]
have been overlayed with residues 39-46 of TAZ2 (yellow) using
the backbone atoms only. The rmsd is 0.43 Å.
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2002,
10,
639-648)
copyright 2002.
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