1wrn
From Proteopedia
(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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| - | [[Image:1wrn.gif|left|200px]]<br /><applet load="1wrn" size=" | + | [[Image:1wrn.gif|left|200px]]<br /><applet load="1wrn" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wrn, resolution 2.30Å" /> | caption="1wrn, resolution 2.30Å" /> | ||
'''Metal Ion dependency of the antiterminator protein, HutP, for binding to the terminator region of hut mRNA- A structural basis'''<br /> | '''Metal Ion dependency of the antiterminator protein, HutP, for binding to the terminator region of hut mRNA- A structural basis'''<br /> | ||
==Overview== | ==Overview== | ||
| - | HutP is an RNA-binding protein that regulates the expression of the | + | 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== | ==About this Structure== | ||
| - | 1WRN 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 MN, HIS and PEG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1WRN 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=MN:'>MN</scene>, <scene name='pdbligand=HIS:'>HIS</scene> and <scene name='pdbligand=PEG:'>PEG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WRN 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.]] | ||
[[Category: Mizuno, H.]] | [[Category: Mizuno, H.]] | ||
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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 15:47:29 2008'' |
Revision as of 13:47, 21 February 2008
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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 , and 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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