1wmq
From Proteopedia
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|PDB= 1wmq |SIZE=350|CAPTION= <scene name='initialview01'>1wmq</scene>, resolution 1.60Å | |PDB= 1wmq |SIZE=350|CAPTION= <scene name='initialview01'>1wmq</scene>, resolution 1.60Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | + | |LIGAND= <scene name='pdbligand=A:ADENOSINE-5'-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=G:GUANOSINE-5'-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=HIS:HISTIDINE'>HIS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=U:URIDINE-5'-MONOPHOSPHATE'>U</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wmq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wmq OCA], [http://www.ebi.ac.uk/pdbsum/1wmq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wmq RCSB]</span> | ||
}} | }} | ||
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[[Category: Kumarevel, T S.]] | [[Category: Kumarevel, T S.]] | ||
[[Category: Mizuno, H.]] | [[Category: Mizuno, H.]] | ||
| - | [[Category: HIS]] | ||
| - | [[Category: MG]] | ||
[[Category: antitermination]] | [[Category: antitermination]] | ||
[[Category: hutp]] | [[Category: hutp]] | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:38:20 2008'' |
Revision as of 21:38, 30 March 2008
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| , resolution 1.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of the HutP antitermination complex bound to a single stranded region of hut mRNA
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
1WMQ 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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