1wpv
From Proteopedia
(New page: 200px<br /><applet load="1wpv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wpv, resolution 1.70Å" /> '''Crystal Structure of...) |
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| - | [[Image:1wpv.gif|left|200px]]<br /><applet load="1wpv" size=" | + | [[Image:1wpv.gif|left|200px]]<br /><applet load="1wpv" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wpv, resolution 1.70Å" /> | caption="1wpv, resolution 1.70Å" /> | ||
'''Crystal Structure of Activated Binary complex of HutP, an RNA binding anti-termination protein'''<br /> | '''Crystal Structure of Activated Binary complex of HutP, an RNA binding anti-termination protein'''<br /> | ||
==Overview== | ==Overview== | ||
| - | HutP regulates the expression of the hut structural genes of Bacillus | + | 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== | ==About this Structure== | ||
| - | 1WPV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with MG and HIS as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1WPV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=HIS:'>HIS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WPV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Kumar, P | + | [[Category: Kumar, P K.R.]] |
| - | [[Category: Kumarevel, T | + | [[Category: Kumarevel, T S.]] |
[[Category: Mizuno, H.]] | [[Category: Mizuno, H.]] | ||
[[Category: HIS]] | [[Category: HIS]] | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:46:56 2008'' |
Revision as of 13:46, 21 February 2008
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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 and 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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