1WMQ

Structure of the HutP antitermination complex bound to a single stranded region of hut mRNA

Summary for 1WMQ

• Entry DOI: 10.2210/pdb1wmq/pdb
• Descriptor: 5'-R(P*UP*UP*UP*AP*GP*UP*U)-3', Hut operon positive regulatory protein, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: hutp, protein-rna complex, antitermination, rna binding, transcription regulation, transcription-rna complex, transcription/rna
• Biological source: Bacillus subtilis
• Total number of polymer chains: 4
• Total formula weight: 36884.21

Authors

Kumarevel, T.S.,Mizuno, H.,Kumar, P.K.R. (deposition date: 2004-07-14, release date: 2005-03-15, Last modification date: 2023-10-25)

Primary citation

Kumarevel, T.,Mizuno, H.,Kumar, P.K.
Structural basis of HutP-mediated anti-termination and roles of the Mg2+ ion and L-histidine ligand.
Nature, 434:183-191, 2005

PubMed Abstract: HutP regulates the expression of the hut structural genes of Bacillus subtilis by an anti-termination mechanism and requires two components, Mg2+ ions and L-histidine. HutP recognizes three UAG triplet units, separated by four non-conserved nucleotides on the terminator region. Here we report the 1.60-A resolution crystal structure of the quaternary complex (HutP-L-histidine-Mg2+-21-base single-stranded RNA). In the complex, the RNA adopts a novel triangular fold on the hexameric surface of HutP, without any base-pairing, and binds to the protein mostly by specific protein-base interactions. The structure explains how the HutP and RNA interactions are regulated critically by the l-histidine and Mg2+ ion through the structural rearrangement. To gain insights into these structural rearrangements, we solved two additional crystal structures (uncomplexed HutP and HutP-L-histidine-Mg2+) that revealed the intermediate structures of HutP (before forming an active structure) and the importance of the Mg2+ ion interactions in the complexes.

PubMed: 15758992
DOI: 10.1038/nature03355

Experimental method

X-RAY DIFFRACTION (1.6 Å)