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PDBsum entry 2f97
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Gene regulation
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PDB id
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2f97
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References listed in PDB file
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Key reference
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Title
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Oligomerization of benm, A lysr-Type transcriptional regulator: structural basis for the aggregation of proteins in this family.
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Authors
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O.C.Ezezika,
S.Haddad,
E.L.Neidle,
C.Momany.
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Ref.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 2007,
63,
361-368.
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PubMed id
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Abstract
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LysR-type transcriptional regulators comprise the largest family of homologous
regulatory DNA-binding proteins in bacteria. A problematic challenge in the
crystallization of LysR-type regulators stems from the insolubility and
precipitation difficulties encountered with high concentrations of the
full-length versions of these proteins. A general oligomerization scheme is
proposed for this protein family based on the structures of the effector-binding
domain of BenM in two different space groups, P4(3)22 and C222(1). These
structures used the same oligomerization scheme of dimer-dimer interactions as
another LysR-type regulator, CbnR, the full-length structure of which is
available [Muraoka et al. (2003), J. Mol. Biol. 328, 555-566]. Evaluation of
packing relationships and surface features suggests that BenM can form infinite
oligomeric arrays in crystals through these dimer-dimer interactions. By
extrapolation to the liquid phase, such dimer-dimer interactions may contribute
to the significant difficulty in crystallizing full-length members of this
family. The oligomerization of dimeric units to form biologically important
tetramers appears to leave unsatisfied oligomerization sites. Under conditions
that favor association, such as neutral pH and concentrations appropriate for
crystallization, higher order oligomerization could cause solubility problems
with purified proteins. A detailed model by which BenM and other LysR-type
transcriptional regulators may form these arrays is proposed.
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Secondary reference #1
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Title
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Crystallization of the effector-Binding domains of benm and catm, Lysr-Type transcriptional regulators from acinetobacter sp. Adp1.
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Authors
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T.Clark,
S.Haddad,
E.Neidle,
C.Momany.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2004,
60,
105-108.
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PubMed id
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