1vea
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vea OCA], [http://www.ebi.ac.uk/pdbsum/1vea PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vea RCSB]</span> | ||
}} | }} | ||
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[[Category: Mizuno, H.]] | [[Category: Mizuno, H.]] | ||
[[Category: Oda, M.]] | [[Category: Oda, M.]] | ||
| - | [[Category: HBN]] | ||
[[Category: antiterminator]] | [[Category: antiterminator]] | ||
[[Category: hutp]] | [[Category: hutp]] | ||
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[[Category: rna binding protein]] | [[Category: rna binding protein]] | ||
| - | ''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 00:23:10 2008'' |
Revision as of 21:23, 30 March 2008
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| , resolution 2.80Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of HutP, an RNA binding antitermination protein
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
1VEA is a Single protein structure of sequence from Bacillus subtilis. 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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