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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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Abstract
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BenM, a member of the LysR-type family of transcriptional regulators, controls
genes for benzoate degradation in the Gram-negative bacterium Acinetobacter sp.
strain ADP1. Recent studies show that BenM activates benABCDE expression
synergistically in response to two effector ligands: cis,cis-muconate (CCM) and
benzoate. As an initial step in investigating the structural basis of dual
effector response, the effector-binding domain of BenM (BenM-EBD) was
crystallized by the microbatch-under-oil technique with conditions optimized
from high-throughput screens performed by the Hauptman-Woodward Institute.
Data-collection quality crystals of BenM-EBD belonged to space group
P2(1)2(1)2(1), diffracted to 2.3 A and had unit-cell parameters a = 65.64, b =
66.34, c = 117.46 A. The influence of effector ligands on crystal formation was
also evaluated. The presence of benzoate or CCM impaired the formation of
crystals. The presence of both effectors together resulted in a dramatic
decrease in the production of crystals. The effector-binding domain of CatM, a
homolog of BenM, was also crystallized.
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