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1vea

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{{STRUCTURE_1vea| PDB=1vea | SCENE= }}
{{STRUCTURE_1vea| PDB=1vea | SCENE= }}
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'''Crystal Structure of HutP, an RNA binding antitermination protein'''
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===Crystal Structure of HutP, an RNA binding antitermination protein===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15242603 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15242603}}
==About this Structure==
==About this Structure==
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==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://www.ncbi.nlm.nih.gov/pubmed/15242603 15242603]
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]
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Crystallization and preliminary X-ray diffraction studies of HutP protein: an RNA-binding protein that regulates the transcription of hut operon in Bacillus subtilis., Kumarevel TS, Fujimoto Z, Padmanabhan B, Oda M, Nishikawa S, Mizuno H, Kumar PK, J Struct Biol. 2002 Jun;138(3):237-40. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12217662 12217662]
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cis-acting regulatory sequences for antitermination in the transcript of the Bacillus subtilis hut operon and histidine-dependent binding of HutP to the transcript containing the regulatory sequences., Oda M, Kobayashi N, Ito A, Kurusu Y, Taira K, Mol Microbiol. 2000 Mar;35(5):1244-54. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10712704 10712704]
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Regulation of transcription]]
[[Category: Regulation of transcription]]
[[Category: Rna binding protein]]
[[Category: Rna binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:28:43 2008''

Revision as of 11:28, 29 July 2008

Template:STRUCTURE 1vea

Crystal Structure of HutP, an RNA binding antitermination protein

Template:ABSTRACT PUBMED 15242603

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

Crystallization and preliminary X-ray diffraction studies of HutP protein: an RNA-binding protein that regulates the transcription of hut operon in Bacillus subtilis., Kumarevel TS, Fujimoto Z, Padmanabhan B, Oda M, Nishikawa S, Mizuno H, Kumar PK, J Struct Biol. 2002 Jun;138(3):237-40. PMID:12217662

cis-acting regulatory sequences for antitermination in the transcript of the Bacillus subtilis hut operon and histidine-dependent binding of HutP to the transcript containing the regulatory sequences., Oda M, Kobayashi N, Ito A, Kurusu Y, Taira K, Mol Microbiol. 2000 Mar;35(5):1244-54. PMID:10712704

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