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Molecular basis of unexpected specificity of ABC transporter-associated substrate-binding protein DppA from .

J. Bacteriol.. 2019; 
RahmanMohammad M,MachucaMayra A,KhanMohammad F,BarlowChristopher K,SchittenhelmRalf B,Roujeinikova
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Bacterial Expression System … (residues 1-22) was codon-optimized for expression in E. coli, synthesized and ligated into the pet151/D-TOPO 348 expression vector (Invitrogen, Waltham, MA, USA) by GenScript. The construct contained an N-terminal His6- 349 … Get A Quote

摘要

The gastric pathogen has limited ability to use carbohydrates as a carbon source, relying instead on exogenous amino acids and peptides. Uptake of certain peptides by requires an ABC transporter annotated dipeptide permease (Dpp). The transporter specificity is determined by its cognate substrate-binding protein DppA that captures ligands in the periplasm and delivers them to the permease. Here, we show that, unlike previously characterized DppA proteins, DppA binds, with micromolar affinity, peptides of diverse amino acid sequences, ranging between two and eight residues in length. We present analysis of the 1.45-Å resolution crystal structure of its complex with the tetrapeptide STSA, whic... More

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