Data of crystal structures of single-domain substrate-binding protein from <i>Rhodothermus marinus</i>.

Abstract

Substrate-binding proteins (SBPs) are essential in ATP-binding cassette transporter systems to determine substrate specificity and delivery. A typical SBP comprises two domains that recognize ligands such as metal ions, amino acids, sugars, and peptides. Interestingly, single-domain SBPs are found in the genomic database, but the molecular function of single-domain SBPs is not fully elucidated. To better understand the molecular function of single-domain SBPs, the crystal structure of single-domain SBPs from <i>Rhodothermus marinus</i> (RmSBP) soaked with NaBr and HgCl₂ were determined at 1.75 and 2.3 Å resolution, respectively. The molecular flexibility of RmSBP and Hg²⁺-bound RmSBP structure was determined. This structural information can be utilized to understand the molecular function of single-domain SBPs. This study reported the detailed process of data collection and structure determination.