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'''Crystal Structure of HutP, an RNA binding anti-termination protein''' | '''Crystal Structure of HutP, an RNA binding anti-termination protein''' | ||
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[[Category: Kumarevel, T S.]] | [[Category: Kumarevel, T S.]] | ||
[[Category: Mizuno, H.]] | [[Category: Mizuno, H.]] | ||
[[Category: | [[Category: Antitermination]] | ||
[[Category: | [[Category: Hutp]] | ||
[[Category: | [[Category: Rna binding]] | ||
[[Category: | [[Category: Transcription regulation]] | ||
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Revision as of 10:59, 3 May 2008
Crystal Structure 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
1WPS is a Single protein structure of sequence from Bacillus subtilis. 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 Page seeded by OCA on Sat May 3 13:59:29 2008
