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PDBsum entry 1e4u
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Gene regulation
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PDB id
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1e4u
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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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The structure of the c4c4 ring finger of human not4 reveals features distinct from those of c3hc4 ring fingers.
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Authors
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H.Hanzawa,
M.J.De ruwe,
T.K.Albert,
P.C.Van der vliet,
H.T.Timmers,
R.Boelens.
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Ref.
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J Biol Chem, 2001,
276,
10185-10190.
[DOI no: ]
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PubMed id
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Abstract
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The NOT4 protein is a component of the CCR4.NOT complex, a global regulator of
RNA polymerase II transcription. Human NOT4 (hNOT4) contains a RING finger motif
of the C(4)C(4) type. We expressed and purified the N-terminal region of hNOT4
(residues 1-78) encompassing the RING finger motif and determined the solution
structure by heteronuclear NMR. NMR experiments using a (113)Cd-substituted
hNOT4 RING finger showed that two metal ions are bound through cysteine residues
in a cross-brace manner. The three-dimensional structure of the hNOT4 RING
finger was refined with root mean square deviation values of 0.58 +/- 0.13 A for
the backbone atoms and 1.08 +/- 0.12 A for heavy atoms. The hNOT4 RING finger
consists of an alpha-helix and three long loops that are stabilized by zinc
coordination. The overall folding of the hNOT4 RING finger is similar to that of
the C(3)HC(4) RING fingers. The relative orientation of the two zinc-chelating
loops and the alpha-helix is well conserved. However, for the other regions, the
secondary structural elements are distinct.
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Figure 3.
Fig. 3. A, superposition of the backbone atoms of 30
simulated annealing structures of hNOT4-N78. The three loop
regions (residues 12-22, 27-38, and 49-61) are colored green;
the region containing the  -helix
(residues 39-48) is in red; residues 23-26 containing the
helical turn are in orange; and the remaining unstructured
region is in white. Zinc atoms are indicated as magenta balls.
B-D, overview of the structural parameters of residues 10-65 of
hNOT4-N78. B, number of distance restraints per residue; C and
D, root mean square deviation (RMSD) for backbone atoms and all
heavy atoms versus the residue number, respectively.
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Figure 5.
Fig. 5. Schematic view of the RING finger structures of
NOT4, IEEHV, RAG1, and c-Cbl. Please note that in RAG1, the
first zinc-binding site of the RING finger is part of the
binuclear zinc cluster. The conserved -helix is
colored red, and the remaining helices and helical turns are in
yellow. The  -sheet is
colored green. Zinc ions are indicated as balls and colored
magenta for conserved zinc and gray for the remaining zinc in
RAG1. Residues that coordinate zinc ions are shown and colored
yellow for cysteine and blue for histidine.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2001,
276,
10185-10190)
copyright 2001.
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