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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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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Transcription regulator
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Title:
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Structure of crga, a lysr-type transcriptional regulator from neisseria meningitidis.
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Structure:
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Transcriptional regulator, lysr family. Chain: a, b, c, d, e, f, g, h. Engineered: yes
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Source:
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Neisseria meningitidis serogroup b. Organism_taxid: 491. Strain: mc58. Gene: crga, nmb1856. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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3.20Å
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R-factor:
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0.218
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R-free:
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0.286
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Authors:
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S.Sainsbury,J.Ren,R.J.Owens,D.I.Stuart,Oxford Protein Production Facility (Oppf)
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Key ref:
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S.Sainsbury
et al.
(2009).
The structure of CrgA from Neisseria meningitidis reveals a new octameric assembly state for LysR transcriptional regulators.
Nucleic Acids Res,
37,
4545-4558.
PubMed id:
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Date:
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15-May-09
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Release date:
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07-Jul-09
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PROCHECK
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Headers
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References
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Q9JXW7
(Q9JXW7_NEIMB) -
Transcriptional regulator, LysR family from Neisseria meningitidis serogroup B (strain MC58)
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Seq:
Struc:
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299 a.a.
293 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Nucleic Acids Res
37:4545-4558
(2009)
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PubMed id:
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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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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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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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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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S.Sainsbury,
J.Ren,
J.E.Nettleship,
N.J.Saunders,
D.I.Stuart,
and
R.J.Owens
(2010).
The structure of a reduced form of OxyR from Neisseria meningitidis.
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BMC Struct Biol,
10,
10.
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PDB code:
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S.Yeom,
J.Yeom,
and
W.Park
(2010).
Molecular characterization of FinR, a novel redox-sensing transcriptional regulator in Pseudomonas putida KT2440.
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Microbiology,
156,
1487-1496.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
