4EYK

Crystal structure of solute binding protein of ABC transporter from Rhodopseudomonas palustris BisB5 in complex with 3,4-dihydroxy benzoic acid

Summary for 4EYK

• Entry DOI: 10.2210/pdb4eyk/pdb
• Related: 4EY3 4EYG
• Descriptor: Twin-arginine translocation pathway signal, 3,4-DIHYDROXYBENZOIC ACID, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: psi-biology, mcsg, midwest center for structural genomics, transporter, lignin degradation product, transport protein
• Biological source: Rhodopseudomonas palustris
• Total number of polymer chains: 1
• Total formula weight: 40199.21

Authors

Chang, C.,Mack, J.,Zerbs, S.,Collart, F.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2012-05-01, release date: 2012-05-30, Last modification date: 2024-10-16)

Primary citation

Michalska, K.,Chang, C.,Mack, J.C.,Zerbs, S.,Joachimiak, A.,Collart, F.R.
Characterization of transport proteins for aromatic compounds derived from lignin: benzoate derivative binding proteins.
J.Mol.Biol., 423:555-575, 2012

PubMed Abstract: In vitro growth experiments have demonstrated that aromatic compounds derived from lignin can be metabolized and represent a major carbon resource for many soil bacteria. However, the proteins that mediate the movement of these metabolites across the cell membrane have not been thoroughly characterized. To address this deficiency, we used a library representative of lignin degradation products and a thermal stability screen to determine ligand specificity for a set of solute-binding proteins (SBPs) from ATP-binding cassette (ABC) transporters. The ligand mapping process identified a set of proteins from Alphaproteobacteria that recognize various benzoate derivatives. Seven high-resolution crystal structures of these proteins in complex with four different aromatic compounds were obtained. The protein-ligand complexes provide details of molecular recognition that can be used to infer binding specificity. This structure-function characterization provides new insight for the biological roles of these ABC transporters and their SBPs, which had been previously annotated as branched-chain amino-acid-binding proteins. The knowledge derived from the crystal structures provides a foundation for development of sequence-based methods to predict the ligand specificity of other uncharacterized transporters. These results also demonstrate that Alphaproteobacteria possess a diverse set of transport capabilities for lignin-derived compounds. Characterization of this new class of transporters improves genomic annotation projects and provides insight into the metabolic potential of soil bacteria.

PubMed: 22925578
DOI: 10.1016/j.jmb.2012.08.017

Experimental method

X-RAY DIFFRACTION (1.9 Å)