Ontology highlight
ABSTRACT:
SUBMITTER: Ruggiero A
PROVIDER: S-EPMC3212476 | biostudies-literature | 2011 Nov
REPOSITORIES: biostudies-literature
Acta crystallographica. Section F, Structural biology and crystallization communications 20111027 Pt 11
The arginine-binding protein from Thermotoga maritima (TmArgBP) is an arginine-binding component of the ATP-binding cassette (ABC) transport system in this hyperthermophilic bacterium. This protein is endowed with an extraordinary stability towards thermal and chemical denaturation. Its structural characterization may provide useful insights for the clarification of structure-stability relationships and for the design of new biosensors. Crystallization trials were set up for both arginine-bound ...[more]