Structural and bioinformatics analysis of single-domain substrate-binding protein from Rhodothermus marinus.

ABSTRACT: Substrate-binding proteins (SBPs) are key elements in determining the substrate specificity and high affinity of the ATP-binding cassette uptake system. A typical SBP has two domains that recognize substrates and are responsible for the specific substrate delivery. Conversely, in GenBank, genes for SBPs constituting a single domain SBP are often found in vicinity of a methyl-accepting chemotaxis protein gene. However, the molecular function and mechanism of single domain SBPs are not fully elucidated. To understand their molecular functions, we performed a crystallographic study of single domain SBP from Rhodothermus marinus (RmSBP). RmSBP crystals were soaked in solution containing NaBr or HgCl₂ and their structures determined at 1.75 and 2.3 Å resolution, respectively.

SUBMITTER: Nam KH 

PROVIDER: S-EPMC10805632 | biostudies-literature | 2024 Mar

REPOSITORIES: biostudies-literature