1vea
From Proteopedia
(New page: 200px<br /><applet load="1vea" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vea, resolution 2.80Å" /> '''Crystal Structure of...) |
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| - | [[Image:1vea.jpg|left|200px]]<br /><applet load="1vea" size=" | + | [[Image:1vea.jpg|left|200px]]<br /><applet load="1vea" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1vea, resolution 2.80Å" /> | caption="1vea, resolution 2.80Å" /> | ||
'''Crystal Structure of HutP, an RNA binding antitermination protein'''<br /> | '''Crystal Structure of HutP, an RNA binding antitermination protein'''<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== | ||
| - | 1VEA 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 HBN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1VEA 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=HBN:'>HBN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VEA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Fujimoto, Z.]] | [[Category: Fujimoto, Z.]] | ||
[[Category: Karthe, P.]] | [[Category: Karthe, P.]] | ||
| - | [[Category: Kumar, P | + | [[Category: Kumar, P K.R.]] |
| - | [[Category: Kumarevel, T | + | [[Category: Kumarevel, T S.]] |
[[Category: Mizuno, H.]] | [[Category: Mizuno, H.]] | ||
[[Category: Oda, M.]] | [[Category: Oda, M.]] | ||
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[[Category: rna binding protein]] | [[Category: rna binding protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:34:21 2008'' |
Revision as of 13:34, 21 February 2008
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Crystal Structure of HutP, an RNA binding antitermination protein
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
1VEA is a Single protein structure of sequence from Bacillus subtilis with as ligand. 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
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