1wrn
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(New page: 200px<br /><applet load="1wrn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wrn, resolution 2.30Å" /> '''Metal Ion dependency...)
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Revision as of 03:30, 21 November 2007
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Metal Ion dependency of the antiterminator protein, HutP, for binding to the terminator region of hut mRNA- A structural basis
Overview
HutP is an RNA-binding protein that regulates the expression of the, histidine utilization (hut) operon in Bacillus subtilis, by binding to, cis-acting regulatory sequences on hut mRNA. It requires L-histidine and, an Mg2+ ion for binding to the specific sequence within the hut mRNA. In, the present study, we show that several divalent cations can mediate the, HutP-RNA interactions. The best divalent cations were Mn2+, Zn2+ and Cd2+, followed by Mg2+, Co2+ and Ni2+, while Cu2+, Yb2+ and Hg2+ were, ineffective. In the HutP-RNA interactions, divalent cations cannot be, replaced by monovalent cations, suggesting that a divalent metal ion is, required for mediating the protein-RNA interactions. To clarify their, importance, we have crystallized HutP in the presence of three different, metal ions (Mg2+, Mn2+ and Ba2+), which revealed the importance of the, metal ion binding site. Furthermore, these analyses clearly demonstrated, how the metal ions cause the structural rearrangements that are required, for the hut mRNA recognition.
About this Structure
1WRN is a Single protein structure of sequence from Bacillus subtilis with MN, HIS and PEG as ligands. Full crystallographic information is available from OCA.
Reference
Characterization of the metal ion binding site in the anti-terminator protein, HutP, of Bacillus subtilis., Kumarevel T, Mizuno H, Kumar PK, Nucleic Acids Res. 2005 Sep 28;33(17):5494-502. Print 2005. PMID:16192572
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