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PDBsum entry 4fb4
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Signaling protein
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PDB id
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4fb4
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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 and functional characterization of solute binding proteins for aromatic compounds derived from lignin: p-Coumaric acid and related aromatic acids.
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Authors
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K.Tan,
C.Chang,
M.Cuff,
J.Osipiuk,
E.Landorf,
J.C.Mack,
S.Zerbs,
A.Joachimiak,
F.R.Collart.
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Ref.
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Proteins, 2013,
81,
1709-1726.
[DOI no: ]
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PubMed id
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Abstract
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Lignin comprises 15-25% of plant biomass and represents a major environmental
carbon source for utilization by soil microorganisms. Access to this energy
resource requires the action of fungal and bacterial enzymes to break down the
lignin polymer into a complex assortment of aromatic compounds that can be
transported into the cells. To improve our understanding of the utilization of
lignin by microorganisms, we characterized the molecular properties of solute
binding proteins of ATP-binding cassette transporter proteins that interact with
these compounds. A combination of functional screens and structural studies
characterized the binding specificity of the solute binding proteins for
aromatic compounds derived from lignin such as p-coumarate, 3-phenylpropionic
acid and compounds with more complex ring substitutions. A ligand screen based
on thermal stabilization identified several binding protein clusters that
exhibit preferences based on the size or number of aromatic ring substituents.
Multiple X-ray crystal structures of protein-ligand complexes for these clusters
identified the molecular basis of the binding specificity for the lignin-derived
aromatic compounds. The screens and structural data provide new functional
assignments for these solute-binding proteins which can be used to infer their
transport specificity. This knowledge of the functional roles and molecular
binding specificity of these proteins will support the identification of the
specific enzymes and regulatory proteins of peripheral pathways that funnel
these compounds to central metabolic pathways and will improve the predictive
power of sequence-based functional annotation methods for this family of
proteins.Proteins 2013; 81:1709-1726. © 2013 Wiley Periodicals, Inc.
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