Crystallographic and microcalorimetric analyses reveal the structural basis for high arginine specificity in the Salmonella enterica serovar Typhimurium periplasmic binding protein STM4351

Publisher:
Wiley-Liss
Publication Type:
Journal Article
Citation:
Proteins: Structure, Function and Genetics, 2011, 79 (7), pp. 2352 - 2357
Issue Date:
2011-01
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Periplasmic binding proteins (PBPs) are crucial transport system components of prokaryotes, required for bacterial growth and survival. PBPs are also used by Gram negative bacteria for small molecule active transport via ATP-binding cassette (ABC) transporters or in signal transduction by inner membrane chemotaxis regulators. Many ligands for PBPs have been identified including amino acids, peptides, vitamins, metal ions, anions, etc. Eight distinct clusters of PBPs have been assigned based on ligand specificity together with amino acid sequence alignments.
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