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Crystallographic and solution structure of the N-terminal domain of the Rel protein from Mycobacterium tuberculosis.
- Source :
-
FEBS letters [FEBS Lett] 2017 Aug; Vol. 591 (15), pp. 2323-2337. Date of Electronic Publication: 2017 Jul 25. - Publication Year :
- 2017
-
Abstract
- Modulation of intracellular guanosine 3',5'-bispyrophosphate ((p)ppGpp) level, the effector of the stringent response, is crucial for survival as well as optimal growth of prokaryotes and, thus, for bacterial pathogenesis and dormancy. In Mycobacterium tuberculosis (Mtb), (p)ppGpp synthesis and degradation are carried out by the bifunctional enzyme MtRel, which consists of 738 residues, including an N-terminal hydrolase- and synthetase-domain (N-terminal domain or NTD) and a C-terminus with a ribosome-binding site. Here, we present the first crystallographic structure of the enzymatically active MtRel NTD determined at 3.7 Å resolution. The structure provides insights into the residues of MtRel NTD responsible for nucleotide binding. Small-angle X-ray scattering experiments were performed to investigate the dimeric state of the MtRel NTD and possible substrate-dependent structural alterations.<br /> (© 2017 Federation of European Biochemical Societies.)
- Subjects :
- Bacterial Proteins genetics
Chromatography, High Pressure Liquid
Crystallography, X-Ray
Ligases chemistry
Ligases genetics
Ligases metabolism
Protein Conformation
Protein Domains
Protein Multimerization
Pyrophosphatases genetics
Scattering, Small Angle
X-Ray Diffraction
Bacterial Proteins chemistry
Bacterial Proteins metabolism
Mycobacterium tuberculosis chemistry
Pyrophosphatases chemistry
Pyrophosphatases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1873-3468
- Volume :
- 591
- Issue :
- 15
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Report
- Accession number :
- 28672070
- Full Text :
- https://doi.org/10.1002/1873-3468.12739