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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Singal B,Balakrishna AM,Nartey W,Manimekalai MSS,Jeyakanthan J,Grüber Gdoi
10.1002/1873-3468.12739subject
Has Abstractpub_date
2017-08-01 00:00:00pages
2323-2337issue
15eissn
0014-5793issn
1873-3468journal_volume
591pub_type
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