1WPS

Crystal Structure of HutP, an RNA binding anti-termination protein

Summary for 1WPS

• Entry DOI: 10.2210/pdb1wps/pdb
• Related: 1VEA 1WMQ 1WPT 1WPU
• Descriptor: Hut operon positive regulatory protein (2 entities in total)
• Functional Keywords: hutp, rna binding, antitermination, transcription regulation, rna binding protein
• Biological source: Bacillus subtilis
• Total number of polymer chains: 2
• Total formula weight: 32202.71

Authors

Kumarevel, T.S.,Mizuno, H.,Kumar, P.K.R. (deposition date: 2004-09-13, 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 (2.8 Å)