3boy: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
[[Image:3boy.jpg|left|200px]]
{{Seed}}
[[Image:3boy.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_3boy|  PDB=3boy  |  SCENE=  }}  
{{STRUCTURE_3boy|  PDB=3boy  |  SCENE=  }}  


'''Crystal structure of the HutP antitermination complex bound to the HUT mRNA'''
===Crystal structure of the HutP antitermination complex bound to the HUT mRNA===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_15242603}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15242603 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_15242603}}


==About this Structure==
==About this Structure==
Line 20: Line 24:
==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]
Identification of important chemical groups of the hut mRNA for HutP interactions that regulate the hut operon in Bacillus subtilis., Kumarevel TS, Gopinath SC, Nishikawa S, Mizuno H, Kumar PK, Nucleic Acids Res. 2004 Jul 25;32(13):3904-12. Print 2004. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15273277 15273277]
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]
Characterization of the metal ion binding site in the anti-terminator protein, HutP, of Bacillus subtilis., Kumarevel T, Mizuno H, Kumar PK, Nucleic Acids Res. 2005 Sep 28;33(17):5494-502. Print 2005. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16192572 16192572]
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Protein complex]]
[[Category: Protein complex]]
Line 42: Line 52:
[[Category: Transcription regulation]]
[[Category: Transcription regulation]]
[[Category: Transcription/rna complex]]
[[Category: Transcription/rna complex]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 20:58:12 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Sep 29 06:12:48 2008''
Retrieved from "https://proteopedia.org/3boy"