1H99

PRD of LicT antiterminator from Bacillus subtilis

Summary for 1H99

• Entry DOI: 10.2210/pdb1h99/pdb
• Descriptor: TRANSCRIPTION ANTITERMINATOR LICT (2 entities in total)
• Functional Keywords: transcriptional antiterminator, pts regulatory domain
• Biological source: BACILLUS SUBTILIS
• Total number of polymer chains: 1
• Total formula weight: 26397.34

Authors

Van Tilbeurgh, H.,Declerck, N. (deposition date: 2001-03-06, release date: 2001-08-28, Last modification date: 2024-05-08)

Primary citation

Van Tilbeurgh, H.,Lecoq, D.,Declerck, N.
Crystal Structure of an Activated Form of the Pts Regulation Domain from the Lict Transcriptional Antitrminator
Embo J., 20:3789-, 2001

PubMed Abstract: The transcriptional antiterminator protein LicT regulates the expression of Bacillus subtilis operons involved in beta-glucoside metabolism. It belongs to a newly characterized family of bacterial regulators whose activity is controlled by the phosphoenolpyruvate:sugar phosphotransferase system (PTS). LicT contains an N-terminal RNA-binding domain (56 residues), and a PTS regulation domain (PRD, 221 residues) that is phosphorylated on conserved histidines in response to substrate availability. Replacement of both His207 and His269 with a negatively charged residue (aspartic acid) led to a highly active LicT variant that no longer responds to either induction or catabolite repression signals from the PTS. In contrast to wild type, the activated mutant form of the LicT regulatory domain crystallized easily and provided the first structure of a PRD, determined at 1.55 A resolution. The structure is a homodimer, each monomer containing two analogous alpha-helical domains. The phosphorylation sites are totally buried at the dimer interface and hence inaccessible to phosphorylating partners. The structure suggests important tertiary and quaternary rearrangements upon LicT activation, which could be communicated from the protein C-terminal end up to the RNA-binding domain.

PubMed: 11447120
DOI: 10.1093/EMBOJ/20.14.3789

Experimental method

X-RAY DIFFRACTION (1.55 Å)