8WGL

Crystal structure of Rhodothermus marinus substrate-binding protein (Hg soaking)

8WGL の概要

• エントリーDOI: 10.2210/pdb8wgl/pdb
• 分子名称: ABC-type uncharacterized transport system periplasmic component-like protein, MERCURY (II) ION (3 entities in total)
• 機能のキーワード: substrate binding protein, transport protein
• 由来する生物種: Rhodothermus marinus DSM 4252
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 41180.52

構造登録者

Nam, K.H. (登録日: 2023-09-22, 公開日: 2023-10-04, 最終更新日: 2024-04-17)

主引用文献

Nam, K.H.
Structural and bioinformatics analysis of single-domain substrate-binding protein from Rhodothermus marinus.
Biochem Biophys Rep, 37:101611-101611, 2024

PubMed 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 (RmSBP). RmSBP crystals were soaked in solution containing NaBr or HgCl and their structures determined at 1.75 and 2.3 Å resolution, respectively. RmSBP soaked in NaBr exhibited disorder of the α2-helix, β5-to β6-strand loop, and C-terminus region, showing the structural dynamic region of RmSBP. RmSBP soaked in HgCl showed that Hg bound to Cys145 located between the α5-and α6-helices. The structural properties of RmSBP were compared with those of single domain SBP homologs. These results will contribute to continued identification of the molecular function and mechanism of single domain SBPs.

PubMed: 38269326
DOI: 10.1016/j.bbrep.2023.101611

実験手法

X-RAY DIFFRACTION (2.3 Å)