1wrn

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|PDB= 1wrn |SIZE=350|CAPTION= <scene name='initialview01'>1wrn</scene>, resolution 2.30&Aring;
|PDB= 1wrn |SIZE=350|CAPTION= <scene name='initialview01'>1wrn</scene>, resolution 2.30&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=HIS:HISTIDINE'>HIS</scene> and <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>
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|LIGAND= <scene name='pdbligand=HIS:HISTIDINE'>HIS</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=[[1vea|1VEA]], [[1wmq|1WMQ]], [[1wps|1WPS]], [[1wpt|1WPT]], [[1wpu|1WPU]], [[1wpv|1WPV]], [[1wro|1WRO]], [[1wrq|1WRQ]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wrn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wrn OCA], [http://www.ebi.ac.uk/pdbsum/1wrn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wrn RCSB]</span>
}}
}}
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[[Category: Kumarevel, T.]]
[[Category: Kumarevel, T.]]
[[Category: Mizuno, H.]]
[[Category: Mizuno, H.]]
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[[Category: HIS]]
 
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[[Category: MN]]
 
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[[Category: PEG]]
 
[[Category: antitermination]]
[[Category: antitermination]]
[[Category: conformational change]]
[[Category: conformational change]]
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[[Category: rna binding protein]]
[[Category: rna binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:00:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:40:06 2008''

Revision as of 21:40, 30 March 2008


PDB ID 1wrn

Drag the structure with the mouse to rotate
, resolution 2.30Å
Ligands: , ,
Related: 1VEA, 1WMQ, 1WPS, 1WPT, 1WPU, 1WPV, 1WRO, 1WRQ


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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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