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

Kalbitzer, H R; Neidig, K P; Hengstenberg, W

doi:10.1021/bi00110a024

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

Full Record
Other Related Research

Abstract

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.

Authors:

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

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

Publication Date:: Tue Nov 19 00:00:00 EST 1991

OSTI Identifier:: 5488395

Resource Type:: Journal Article

Journal Name:: Biochemistry; (United States)

Additional Journal Information:: Journal Volume: 30:46; Journal ID: ISSN 0006-2960

Country of Publication:: United States

Language:: English

Subject:: 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

Citation Formats


                    Kalbitzer, H R, Neidig, K P, and Hengstenberg, W. Two-dimensional sup 1 H NMR studies on HPr protein from Staphylococcus aureus: Complete sequential assignments and secondary structure.  United States: N. p., 1991. 
        Web.  doi:10.1021/bi00110a024.

Copy to clipboard


                    Kalbitzer, H R, Neidig, K P, & Hengstenberg, W. Two-dimensional sup 1 H NMR studies on HPr protein from Staphylococcus aureus: Complete sequential assignments and secondary structure.  United States.  https://doi.org/10.1021/bi00110a024

Copy to clipboard


                    Kalbitzer, H R, Neidig, K P, and Hengstenberg, W. 1991.  
        "Two-dimensional sup 1 H NMR studies on HPr protein from Staphylococcus aureus: Complete sequential assignments and secondary structure".  United States.  https://doi.org/10.1021/bi00110a024.

Copy to clipboard


                    
@article{osti_5488395,

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

  author       = {Kalbitzer, H R and Neidig, K P and Hengstenberg, W},

  abstractNote = {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.},

  doi          = {10.1021/bi00110a024},

  url          = {https://www.osti.gov/biblio/5488395},
  journal      = {Biochemistry; (United States)},

  issn         = {0006-2960},

  number       = ,

  volume       = 30:46,

  place        = {United States},

  year         = {Tue Nov 19 00:00:00 EST 1991},

  month        = {Tue Nov 19 00:00:00 EST 1991}

}

Copy to clipboard

Journal Article:

https://doi.org/10.1021/bi00110a024

Other availability

Find in Google Scholar

Search WorldCat to find libraries that may hold this journal

Save / Share:

Export Metadata

Save to My Library

Similar records in OSTI.GOV collections:

Sequence-specific sup 1 H NMR resonance assignments of Bacillus subtilis HPr: Use of spectra obtained from mutants to resolve spectral overlap

Journal Article Wittekind, M; Klevit, R; Reizer, J - Biochemistry; (USA)

On the basis of an analysis of two-dimensional {sup 1}H NMR spectra, the complete sequence-specific {sup 1}H NMR assignments are presented for the phosphocarrier protein HPr from the Gram-positive bacterium Bacillus subtilis. During the assignment procedure, extensive use was made of spectra obtained from point mutants of HPr in order to resolve spectral overlap and to provide verification of assignments. Regions of regular secondary structure were identified by characteristic patterns of sequential backbone proton NOEs and slowly exchanging amide protons. B subtilis HPr contains four {beta}-strands that form a single antiparallel {beta}-sheet and two well-defined {alpha}-helices. There are two stretchesmore »« less
https://doi.org/10.1021/bi00483a006
Staphylococcal phosphoenolpyruvate-dependent phosphotransferase system: purification and characterization of the mannitol-specific enzyme III/sup mtl/ of Staphylococcus aureus and Staphylococcus carnosus and homology with the enzyme II/sup mtl/ of Escherichia coli

Journal Article Reiche, B; Frank, R; Deutscher, J; ... - Biochemistry; (United States)

Enzyme III/sup mtl/ is part of the mannitol phosphotransferase system of Staphylococcus aureus and Staphylococcus carnosus and is phosphorylated by phosphoenolpyruvate in a reaction sequence requiring enzyme I (phosphoenolpyruvate-protein phosphotransferase) and the histidine-containing protein HPr. In this paper, the authors report the isolation of III/sup mtl/ from both S. aureus and S. carnosus and the characterization of the active center. After phosphorylation of III/sup mtl/ with (/sup 32/P)PEP, enzyme I, and HPr, the phosphorylated protein was cleaved with endoproteinase GLu(C). The amino acid sequence of the S. aureus peptide carrying the phosphoryl group was found to be Gln-Val-Val-Ser-Thr-Phe-Met-Gly-Asn-Gly-Leu-Ala-Ile-Pro-His-Gly-Thr-Asp-Asp. The correspondingmore »« less
Polypeptide backbone resonance assignments and secondary structure of Bacillus subtilis enzyme III sup glc determined by two-dimensional and three-dimensional heteronuclear NMR spectroscopy

Journal Article Fairbrother, W; Cavanagh, J; Dyson, H; ... - Biochemistry; (United States)

The enzyme III{sup glc}-like domain of Bacillus subtilis II{sup glc} (III{sup glc}; 162 residues, 17.4 kDa) has been cloned and overexpressed in Escherichia coli. Sequence-specific assignment of the backbone {sup 1}H and {sup 15}N resonances has been carried out with a combination of mohonuclear and heteronuclear two-dimensional and heteronuclear three-dimensional (3D) NMR spectroscopy. Amide proton solvent exchange rate constants have been determined from a series of {sup 1}H-{sup 15}N heteronuclear single-quantum coherence (HSQC) spectra acquired following dissolution of the protein in D{sub 2}O. Major structural features of III{sup glc} have been inferred from the pattern of short-, medium- and long-rangemore »« less
https://doi.org/10.1021/bi00242a013
Comparison of killing of gram-negative and gram-positive bacteria by pure singlet oxygen. [Salmonella typhimurium; Escherichia coli; Sarcina lutea; Staphylococcus aureus; Streptococcus lactis; Streptococcus faecalis]

Journal Article Dahl, T; Midden, W; Hartman, P - Journal of Bacteriology; (USA)

Gram-negative and gram-positive bacteria were found to display different sensitivities to pure singlet oxygen generated outside of cells. Killing curves for Salmonella typhimurium and Escherichia coli strains were indicative of multihit killing, whereas curves for Sarcina lutea, Staphylococcus aureus, Streptococcus lactis, and Streptococcus faecalis exhibited single-hit kinetics. The S. typhimurium deep rough strain TA1975, which lacks nearly all of the cell wall lipopolysaccharide coat and manifests concomitant enhancement of penetration by some exogenous substances, responded to singlet oxygen with initially faster inactivation than did the S. typhimurium wild-type strain, although the maximum rates of killing appeared to be quite similar.more »« less
Secondary structure of the phosphocarrier protein III sup Glc , a signal-transducing protein from Escherichia coli, determined by heteronuclear three-dimensional NMR spectroscopy

Journal Article Pelton, J; Torchia, D; Meadow, N; ... - Proceedings of the National Academy of Sciences of the United States of America; (United States)

III{sup Glc} is signal-transducing phosphocarrier protein of the phosphoenolpyruvate:glycose phosphotransferase system of Escherichia coli. The secondary structure of III{sup Glc} is determined by heteronuclear ({sup 15}N, {sup 13}C) three-dimensional NMR spectroscopy. Sequential, medium-range, and long-range nuclear Overhauser effects seen in NMR spectra are used to elucidate 11 antiparallel {beta}-strands and four helical segments. The medium-range nuclear Overhauser effect patterns suggest that the helices are either distorted {alpha}-helices or are of the 3{sub 10} class. The amino acids separating the active-site histidine residues (His{sup 75} and His{sup 90}) form two strands (Ala{sup 76}-Ser{sup 81} and Val{sup 85}-Phe{sup 91}) of a six-strandedmore »« less
https://doi.org/10.1073/pnas.88.8.3479

Similar Records