The solution structure of the histidine‐containing protein (HPr) from Staphylococcus aureus as determined by two‐dimensional 1H‐NMR spectroscopy

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Abstract
The three‐dimensional solution structure of the heat‐stable phosphocarrier protein HPr from Staphylococcus aureus was determined from two‐dimensional NMR data by restrained molecular dynamics. It consists of a large twisted antiparallel β‐pleated sheet with four strands A, B, C, and D of amino acids 2–7, 34–37, 40–42 and 60–65. Three right‐handed helices A, B, C (amino acids 18–27, 47–53 and 71–85) are positioned on top of this sheet. The aromatic ring of His15 is located in a cleft formed by amino acids 12–17 and 55–58, only the nitrogen (Nδ1) atom which can be phosphorylated by enzyme I is exposed to the water. The side chains of Thr12 and Arg17 are located close to the histidine ring. The regulatory serine residue (Ser46) is located in a hydrophobic patch, its hydroxyl group is water‐accessible but forms hydrogen bonds with the amide groups of the backbone. The general features of the three‐dimensional structure are similar to those found in HPr proteins from different microorganisms such as Escherichia coli, Bacillus subtilis and Streptococcus faecalis.