2024
DOI: 10.1016/j.bbrep.2023.101611
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Structural and bioinformatics analysis of single-domain substrate-binding protein from Rhodothermus marinus

Ki Hyun Nam
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“…Typical SBP proteins recognize a substrate using two α/β domains [12] , whereas the single-domain substrate-binding protein from Rhodothermus marinus (RmSBP) has a single α/β domain. The crystal structure and flexibility of RmSBP have been established [12] , [13] , [14] , but its molecular function is unknown. To better understand this process, radiation damage to selenomethionine-substituted RmSBP (SeMet-RmSBP) was used as a model sample, rather than focusing on the identification of biological function [1] .…”
Section: Introductionmentioning
confidence: 99%
“…Typical SBP proteins recognize a substrate using two α/β domains [12] , whereas the single-domain substrate-binding protein from Rhodothermus marinus (RmSBP) has a single α/β domain. The crystal structure and flexibility of RmSBP have been established [12] , [13] , [14] , but its molecular function is unknown. To better understand this process, radiation damage to selenomethionine-substituted RmSBP (SeMet-RmSBP) was used as a model sample, rather than focusing on the identification of biological function [1] .…”
Section: Introductionmentioning
confidence: 99%