1vea
From Proteopedia
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| - | [[Image:1vea.jpg|left|200px]] | + | [[Image:1vea.jpg|left|200px]] |
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| - | '''Crystal Structure of HutP, an RNA binding antitermination protein''' | + | {{Structure |
| + | |PDB= 1vea |SIZE=350|CAPTION= <scene name='initialview01'>1vea</scene>, resolution 2.80Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=HBN:N-(2-NAPHTHYL)HISTIDINAMIDE'>HBN</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of HutP, an RNA binding antitermination protein''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1VEA is a [ | + | 1VEA 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=1VEA OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15242603 15242603] |
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: rna binding protein]] | [[Category: rna binding protein]] | ||
| - | ''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 14:44:22 2008'' |
Revision as of 12:44, 20 March 2008
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| 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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