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

Journal Article · Tue Aug 07 04:00:00 EDT 1990 · Biochemistry; (USA)

DOI:https://doi.org/10.1021/bi00483a006· OSTI ID:6058374

Wittekind, M; Klevit, R E ^[1]; Reizer, J ^[2]

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1. Univ. of Washington, Seattle (USA)
2. Univ. of California, San Diego (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 stretches of extended backbone structure, one of which contains the active site His{sub 15}. The overall fold of the protein is very similar to that of Escherichia coli HPr determined by NMR studies.

• OSTI ID: 6058374
• Journal Information: Biochemistry; (USA), Journal Name: Biochemistry; (USA) Vol. 29:31; ISSN 0006-2960; ISSN BICHA
• Country of Publication: United States
• Language: English

Related Subjects

550601* -- Medicine-- Unsealed Radionuclides in Diagnostics
62 RADIOLOGY AND NUCLEAR MEDICINE
BACILLUS
BACILLUS SUBTILIS
BACTERIA
BARYONS
CHEMICAL SHIFT
DEUTERIUM COMPOUNDS
ELEMENTARY PARTICLES
ESCHERICHIA COLI
FERMIONS
HADRONS
HYDROGEN COMPOUNDS
MAGNETIC RESONANCE
MEMBRANE PROTEINS
MICROORGANISMS
NMR SPECTRA
NUCLEAR MAGNETIC RESONANCE
NUCLEONS
ORGANIC COMPOUNDS
PROTEINS
PROTONS
PURIFICATION
RESONANCE
SPECTRA