1wpv
From Proteopedia
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Crystal Structure of Activated Binary complex of HutP, an RNA binding anti-termination protein
Overview
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.
About this Structure
1WPV is a Single protein structure of sequence from Bacillus subtilis with MG and HIS as ligands. Full crystallographic information is available from OCA.
Reference
Structural basis of HutP-mediated anti-termination and roles of the Mg2+ ion and L-histidine ligand., Kumarevel T, Mizuno H, Kumar PK, Nature. 2005 Mar 10;434(7030):183-91. PMID:15758992
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