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PDBsum entry 3hhg
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Transcription regulator
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PDB id
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3hhg
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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 crga from neisseria meningitidis reveals a new octameric assembly state for lysr transcriptional regulators.
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Authors
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S.Sainsbury,
L.A.Lane,
J.Ren,
R.J.Gilbert,
N.J.Saunders,
C.V.Robinson,
D.I.Stuart,
R.J.Owens.
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Ref.
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Nucleic Acids Res, 2009,
37,
4545-4558.
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PubMed id
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Abstract
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LysR-type transcriptional regulators (LTTRs) form the largest family of
bacterial regulators acting as both auto-repressors and activators of target
promoters, controlling operons involved in a wide variety of cellular processes.
The LTTR, CrgA, from the human pathogen Neisseria meningitidis, is upregulated
during bacterial-host cell contact. Here, we report the crystal structures of
both regulatory domain and full-length CrgA, the first of a novel subclass of
LTTRs that form octameric rings. Non-denaturing mass spectrometry analysis and
analytical ultracentrifugation established that the octameric form of CrgA is
the predominant species in solution in both the presence and absence of an
oligonucleotide encompassing the CrgA-binding sequence. Furthermore, analysis of
the isolated CrgA-DNA complex by mass spectrometry showed stabilization of a
double octamer species upon DNA binding. Based on the observed structure and the
mass spectrometry findings, a model is proposed in which a hexadecameric array
of two CrgA oligomers binds to its DNA target site.
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