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Structural basis of HutP-mediated anti-termination and roles of the Mg2+ ion and L-histidine ligand | | Thirumananseri Kumarevel
; Hiroshi Mizuno
; Penmetcha K R Kumar
; | | Date: |
10 Mar 2005 | | Journal: | Nature, 434 (7030), 183-91 | | 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. | | Source: | PubMed, pmid15758992 doi: 10.1038/nature03355 | | Services: | Forum | Review | Favorites | |
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