8WGL
Crystal structure of Rhodothermus marinus substrate-binding protein (Hg soaking)
Summary for 8WGL
| Entry DOI | 10.2210/pdb8wgl/pdb |
| Descriptor | ABC-type uncharacterized transport system periplasmic component-like protein, MERCURY (II) ION (3 entities in total) |
| Functional Keywords | substrate binding protein, transport protein |
| Biological source | Rhodothermus marinus DSM 4252 |
| Total number of polymer chains | 2 |
| Total formula weight | 41180.52 |
| Authors | Nam, K.H. (deposition date: 2023-09-22, release date: 2023-10-04, Last modification date: 2024-04-17) |
| Primary citation | Nam, K.H. Structural and bioinformatics analysis of single-domain substrate-binding protein from Rhodothermus marinus. Biochem Biophys Rep, 37:101611-101611, 2024 Cited by 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: 38269326DOI: 10.1016/j.bbrep.2023.101611 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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