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3boy

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(New page: 200px<br /><applet load="3boy" size="350" color="white" frame="true" align="right" spinBox="true" caption="3boy, resolution 1.70&Aring;" /> '''Crystal structure of...)
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==Overview==
==Overview==
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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.
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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==
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3BOY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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]. This structure superseeds the now removed PDB entry 2GZT. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BOY OCA].
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3BOY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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]. This structure supersedes the now removed PDB entry 2GZT. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BOY OCA].
==Reference==
==Reference==
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[[Category: Balasundaresan, D.]]
[[Category: Balasundaresan, D.]]
[[Category: Jeyakanthan, J.]]
[[Category: Jeyakanthan, J.]]
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[[Category: Kumar, P.K.R.]]
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[[Category: Kumar, P K.R.]]
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[[Category: Kumarevel, T.S.]]
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[[Category: Kumarevel, T S.]]
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[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
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[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: Shinkai, A.]]
[[Category: Shinkai, A.]]
[[Category: Yokoyama, S.]]
[[Category: Yokoyama, S.]]
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[[Category: transcription/rna complex]]
[[Category: transcription/rna complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:11:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:06:49 2008''

Revision as of 17:06, 21 February 2008


3boy, resolution 1.70Å

Drag the structure with the mouse to rotate

Crystal structure of the HutP antitermination complex bound to the 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

3BOY is a Protein complex structure of sequences from Bacillus subtilis with and as ligands. This structure supersedes the now removed PDB entry 2GZT. 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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