Two-dimensional sup 1 H NMR studies on HPr protein from Staphylococcus aureus: Complete sequential assignments and secondary structure

Journal Article · Tue Nov 19 04:00:00 EST 1991 · Biochemistry; (United States)

DOI:https://doi.org/10.1021/bi00110a024· OSTI ID:5488395

Kalbitzer, H R; Neidig, K P ^[1]; Hengstenberg, W ^[2]

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1. Max-Planck-Inst. for Medical Research, Heidelberg (West Germany)
2. Univ. of Bochum (West Germany)

Complete sequence-specific assignments of the {sup 1}H 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 S{sub AB} 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 S{sub CD} which shows no typical secondary structure, and the {alpha}-helical, C-terminal segment S{sub 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.

• OSTI ID: 5488395
• Journal Information: Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 30:46; ISSN 0006-2960; ISSN BICHA
• Country of Publication: United States
• Language: English

Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
BACTERIA
BARYONS
ELEMENTARY PARTICLES
ENZYMES
ESCHERICHIA COLI
FERMIONS
HADRONS
MAGNETIC RESONANCE
MICROORGANISMS
MOLECULAR STRUCTURE
NUCLEAR MAGNETIC RESONANCE
NUCLEONS
ORGANIC COMPOUNDS
OVERHAUSER EFFECT
PHOSPHORUS-GROUP TRANSFERASES
PHOSPHOTRANSFERASES
PROTEINS
PROTONS
RESONANCE
STAPHYLOCOCCUS
STREPTOCOCCUS
TRANSFERASES