Common structural changes accompany the functional inactivation of HPr by seryl phosphorylation or by serine to aspartate substitution

Journal Article · Tue Dec 26 00:00:00 EST 1989 · Biochemistry; (USA)

DOI:https://doi.org/10.1021/bi00452a005· OSTI ID:6921110

Wittekind, M; Klevit, R E ^[1]; Reizer, J; Saier, M H ^[2]; Deutscher, J ^[3]

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1. Univ. of Washington, Seattle (USA)
2. Univ. of California, La Jolla (USA)
3. Max-Planck-Institut fuer Systemphysiologie, Dortmund (West Germany)

Although many proteins are known to be regulated via reversible phosphorylation, little is known about the mechanism by which the covalent modification of seryl, threonyl, or tyrosyl residues alters the activities of the target systems. To address this question, modified versions of bacillus subtilus HPr, a protein component of the bacterial phosphotransferase system, have been studied by {sup 1}H NMR spectroscopy. Phosphorylation at Ser{sub 46} or a Ser to Asp substitution at this position inactivates HPr. Two-dimensional spectra of these two modified proteins display nearly identical proton chemical shifts that differ significantly from those observed in the spectra of the unphosphorylated, wild-type protein and of functionally active HPr mutants. These results demonstrate that the functional inactivation of HPr brought about by the serine to aspartate mutation is accompanied by the same structural changes that occur when HPr is phosphorylated at Ser{sub 46}.

• OSTI ID: 6921110
• Journal Information: Biochemistry; (USA), Vol. 28:26; ISSN 0006-2960
• Country of Publication: United States
• Language: English

Related Subjects

62 RADIOLOGY AND NUCLEAR MEDICINE
PHOSPHOTRANSFERASES
NUCLEAR MAGNETIC RESONANCE
ASPARTIC ACID
BACILLUS SUBTILIS
INACTIVATION
MOLECULAR STRUCTURE
NMR SPECTRA
PHOSPHORYLATION
PROTONS
SERINE
AMINO ACIDS
BACILLUS
BACTERIA
BARYONS
CARBOXYLIC ACIDS
CHEMICAL REACTIONS
ELEMENTARY PARTICLES
ENZYMES
FERMIONS
HADRONS
HYDROXY ACIDS
MAGNETIC RESONANCE
MICROORGANISMS
NUCLEONS
ORGANIC ACIDS
ORGANIC COMPOUNDS
PHOSPHORUS-GROUP TRANSFERASES
RESONANCE
SPECTRA
TRANSFERASES
550601* - Medicine- Unsealed Radionuclides in Diagnostics