Two-dimensional proton NMR studies on HPr protein from Staphylococcus aureus: complete sequential assignments and secondary structure

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Abstract
Complete sequence-specific assignments of the 1H NMR spectrum of HPr protein from Staphylococcus aureus were obtained by two-dimensional NMR methods. Important secondary structure elements that can be derived from the observed nuclear Overhauser effects are a large antiparallel beta-pleated sheet consisting of four strands, A, B, C, D, a segment SAB consisting of an extended region around the active-center histidine (His-15) and an alpha-helix, a half-turn between strands B and C, a segment SCD which shows no typical secondary structure, and the alpha-helical, C-terminal segment S(term). These general structural features are similar to those found earlier in HPr proteins from different microorganisms such as Escherichia coli, Bacillus subtilis, and Streptococcus faecalis.

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