1wpv: Difference between revisions
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[[Image:1wpv.gif|left|200px]] | [[Image:1wpv.gif|left|200px]] | ||
'''Crystal Structure of Activated Binary complex of HutP, an RNA binding anti-termination protein''' | {{Structure | ||
|PDB= 1wpv |SIZE=350|CAPTION= <scene name='initialview01'>1wpv</scene>, resolution 1.70Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=HIS:HISTIDINE'>HIS</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal Structure of Activated Binary complex of HutP, an RNA binding anti-termination protein''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1WPV is a [ | 1WPV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WPV OCA]. | ||
==Reference== | ==Reference== | ||
Structural basis of HutP-mediated anti-termination and roles of the Mg2+ ion and L-histidine ligand., Kumarevel T, Mizuno H, Kumar PK, Nature. 2005 Mar 10;434(7030):183-91. PMID:[http:// | Structural basis of HutP-mediated anti-termination and roles of the Mg2+ ion and L-histidine ligand., Kumarevel T, Mizuno H, Kumar PK, Nature. 2005 Mar 10;434(7030):183-91. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15758992 15758992] | ||
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:00:06 2008'' | ||
Revision as of 13:00, 20 March 2008
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| 1wpv, resolution 1.70Å | |||||||||||||
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| Ligands: | MG and HIS | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Crystal Structure of Activated Binary complex of HutP, an RNA binding anti-termination protein
Overview
HutP regulates the expression of the hut structural genes of Bacillus subtilis by an anti-termination mechanism and requires two components, Mg2+ ions and L-histidine. HutP recognizes three UAG triplet units, separated by four non-conserved nucleotides on the terminator region. Here we report the 1.60-A resolution crystal structure of the quaternary complex (HutP-L-histidine-Mg2+-21-base single-stranded RNA). In the complex, the RNA adopts a novel triangular fold on the hexameric surface of HutP, without any base-pairing, and binds to the protein mostly by specific protein-base interactions. The structure explains how the HutP and RNA interactions are regulated critically by the l-histidine and Mg2+ ion through the structural rearrangement. To gain insights into these structural rearrangements, we solved two additional crystal structures (uncomplexed HutP and HutP-L-histidine-Mg2+) that revealed the intermediate structures of HutP (before forming an active structure) and the importance of the Mg2+ ion interactions in the complexes.
About this Structure
1WPV is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Structural basis of HutP-mediated anti-termination and roles of the Mg2+ ion and L-histidine ligand., Kumarevel T, Mizuno H, Kumar PK, Nature. 2005 Mar 10;434(7030):183-91. PMID:15758992
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