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

Journal Article · Tue Nov 19 00:00:00 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), Vol. 30:46; ISSN 0006-2960
• Country of Publication: United States
• Language: English

Related Subjects

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