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PDBsum entry 2vus
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Transcription
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PDB id
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2vus
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Contents |
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(+ 2 more)
318 a.a.
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42 a.a.
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43 a.a.
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References listed in PDB file
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Key reference
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Title
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Structural analysis of the recognition of the negative regulator nmra and DNA by the zinc finger from the gata-Type transcription factor area.
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Authors
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M.Kotaka,
C.Johnson,
H.K.Lamb,
A.R.Hawkins,
J.Ren,
D.K.Stammers.
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Ref.
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J Mol Biol, 2008,
381,
373-382.
[DOI no: ]
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PubMed id
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Abstract
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Amongst the most common protein motifs in eukaryotes are zinc fingers (ZFs),
which, although largely known as DNA binding modules, also can have additional
important regulatory roles in forming protein:protein interactions. AreA is a
transcriptional activator central to nitrogen metabolism in Aspergillus
nidulans. AreA contains a GATA-type ZF that has a competing dual recognition
function, binding either DNA or the negative regulator NmrA. We report the
crystal structures of three AreA ZF-NmrA complexes including two with bound
NAD(+) or NADP(+). The molecular recognition of AreA ZF-NmrA involves binding of
the ZF to NmrA via hydrophobic and hydrogen bonding interactions through helices
alpha1, alpha6 and alpha11. Comparison with an earlier NMR solution structure of
AreA ZF-DNA complex by overlap of the AreA ZFs shows that parts of helices
alpha6 and alpha11 of NmrA are positioned close to the GATA motif of the DNA,
mimicking the major groove of DNA. The extensive overlap of DNA with NmrA
explains their mutually exclusive binding to the AreA ZF. The presence of bound
NAD(+)/NADP(+) in the NmrA-AreaA ZF complex, however, causes minimal structural
changes. Thus, any regulatory effects on AreA function mediated by the binding
of oxidised nicotinamide dinucleotides to NmrA in the NmrA-AreA ZF complex
appear not to be modulated via protein conformational rearrangements.
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Figure 1.
Fig. 1. (a) Orthogonal views of the NmrA–AreA ZF complex in
stereo. NmrA (white) is shown with NAD^+ bound. AreA ZF is shown
in red, and the α-helices of NmrA involved in AreA interaction
are highlighted in yellow and labelled. (b) Simulated annealing
omit difference map of residues 702 to 712 of AreA ZF at σ =
2.5. The carbon atoms are drawn in black.
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Figure 2.
Fig. 2. Stereo representations of the NmrA–AreA ZF binding
interface. (a) Interaction between the C-terminal tail of AreA
ZF (cyan) and NmrA helix α6 (yellow). (b) Interaction between
the AreA ZF protein core (cyan) and NmrA helix α11 (yellow).
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2008,
381,
373-382)
copyright 2008.
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