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[[Image:1wpu.gif|left|200px]]


{{Structure
==Crystal Structure of the HutP antitermination complex bound to a single stranded region of hut mRNA==
|PDB= 1wpu |SIZE=350|CAPTION= <scene name='initialview01'>1wpu</scene>, resolution 1.48&Aring;
<StructureSection load='1wpu' size='340' side='right'caption='[[1wpu]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=A:ADENOSINE-5&#39;-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=G:GUANOSINE-5&#39;-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=HIS:HISTIDINE'>HIS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=U:URIDINE-5&#39;-MONOPHOSPHATE'>U</scene>
<table><tr><td colspan='2'>[[1wpu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WPU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WPU FirstGlance]. <br>
|ACTIVITY=
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.48&#8491;</td></tr>
|GENE=
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HIS:HISTIDINE'>HIS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wpu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wpu OCA], [https://pdbe.org/1wpu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wpu RCSB], [https://www.ebi.ac.uk/pdbsum/1wpu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wpu ProSAT]</span></td></tr>
|RELATEDENTRY=[[1vea|1VEA]], [[1wmq|1WMQ]], [[1wps|1WPS]], [[1wpt|1WPT]], [[1wpv|1WPV]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wpu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wpu OCA], [http://www.ebi.ac.uk/pdbsum/1wpu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wpu RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/HUTP_BACSU HUTP_BACSU] Antiterminator that binds to cis-acting regulatory sequences on the mRNA in the presence of histidine, thereby suppressing transcription termination and activating the hut operon for histidine utilization.[HAMAP-Rule:MF_00779]
 
== Evolutionary Conservation ==
'''Crystal Structure of the HutP antitermination complex bound to a single stranded region of hut mRNA'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wp/1wpu_consurf.spt"</scriptWhenChecked>
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.
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==About this Structure==
  </jmolCheckbox>
1WPU 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=1WPU OCA].  
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1wpu ConSurf].
 
<div style="clear:both"></div>
==Reference==
__TOC__
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]
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Kumar, P K.R.]]
[[Category: Kumar PKR]]
[[Category: Kumarevel, T S.]]
[[Category: Kumarevel TS]]
[[Category: Mizuno, H.]]
[[Category: Mizuno H]]
[[Category: antitermination]]
[[Category: hutp]]
[[Category: hutp-rna complex]]
[[Category: rna binding]]
[[Category: transcription regulation]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:39:29 2008''
Retrieved from "https://proteopedia.org/1wpu"