1wpu
From Proteopedia
(New page: 200px<br /><applet load="1wpu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wpu, resolution 1.48Å" /> '''Crystal Structure of...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1wpu.gif|left|200px]]<br /><applet load="1wpu" size=" | + | [[Image:1wpu.gif|left|200px]]<br /><applet load="1wpu" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wpu, resolution 1.48Å" /> | caption="1wpu, resolution 1.48Å" /> | ||
'''Crystal Structure of the HutP antitermination complex bound to a single stranded region of hut mRNA'''<br /> | '''Crystal Structure of the HutP antitermination complex bound to a single stranded region of hut mRNA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | HutP is an L-histidine-activated RNA binding protein that regulates the | + | HutP is an L-histidine-activated RNA binding protein that regulates the expression of the histidine utilization (hut) operon in Bacillus subtilis by binding to cis-acting regulatory sequences on the hut mRNA. The crystal structure of HutP complexed with an L-histidine analog showed a novel fold; there are four antiparallel beta strands in the central region of each monomer, with two alpha helices each on the front and back. Two HutP monomers form a dimer, and three dimers are arranged in crystallographic 3-fold symmetry to form a hexamer. A histidine analog was located in between the two monomers of HutP, with the imidazole group of L-histidine hydrogen bonded to Glu81. An activation mechanism is proposed based on the identification of key residues of HutP. The HutP binding region in hut mRNA was defined: it consists of three UAG trinucleotide motifs separated by four spacer nucleotides. Residues of HutP potentially important for RNA binding were identified. |
==About this Structure== | ==About this Structure== | ||
| - | 1WPU 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:// | + | 1WPU 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=1WPU OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[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]] | ||
| Line 24: | Line 24: | ||
[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:46:57 2008'' |
Revision as of 13:46, 21 February 2008
|
Crystal Structure of the HutP antitermination complex bound to a single stranded region of hut mRNA
Overview
HutP is an L-histidine-activated RNA binding protein that regulates the expression of the histidine utilization (hut) operon in Bacillus subtilis by binding to cis-acting regulatory sequences on the hut mRNA. The crystal structure of HutP complexed with an L-histidine analog showed a novel fold; there are four antiparallel beta strands in the central region of each monomer, with two alpha helices each on the front and back. Two HutP monomers form a dimer, and three dimers are arranged in crystallographic 3-fold symmetry to form a hexamer. A histidine analog was located in between the two monomers of HutP, with the imidazole group of L-histidine hydrogen bonded to Glu81. An activation mechanism is proposed based on the identification of key residues of HutP. The HutP binding region in hut mRNA was defined: it consists of three UAG trinucleotide motifs separated by four spacer nucleotides. Residues of HutP potentially important for RNA binding were identified.
About this Structure
1WPU is a Single protein structure of sequence from Bacillus subtilis with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of activated HutP; an RNA binding protein that regulates transcription of the hut operon in Bacillus subtilis., Kumarevel T, Fujimoto Z, Karthe P, Oda M, Mizuno H, Kumar PK, Structure. 2004 Jul;12(7):1269-80. PMID:15242603
Page seeded by OCA on Thu Feb 21 15:46:57 2008
