3boy

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==Crystal structure of the HutP antitermination complex bound to the HUT mRNA==
==Crystal structure of the HutP antitermination complex bound to the HUT mRNA==
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<StructureSection load='3boy' size='340' side='right' caption='[[3boy]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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<StructureSection load='3boy' size='340' side='right'caption='[[3boy]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3boy]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2gzt 2gzt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BOY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BOY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3boy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2gzt 2gzt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BOY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BOY FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HIS:HISTIDINE'>HIS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vea|1vea]], [[1wpt|1wpt]], [[1wmq|1wmq]], [[1wpu|1wpu]], [[1wrq|1wrq]], [[1wpv|1wpv]]</td></tr>
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<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>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hutP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Bacillus globigii" Migula 1900])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3boy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3boy OCA], [https://pdbe.org/3boy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3boy RCSB], [https://www.ebi.ac.uk/pdbsum/3boy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3boy ProSAT], [https://www.topsan.org/Proteins/RSGI/3boy TOPSAN]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3boy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3boy OCA], [http://pdbe.org/3boy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3boy RCSB], [http://www.ebi.ac.uk/pdbsum/3boy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3boy ProSAT], [http://www.topsan.org/Proteins/RSGI/3boy TOPSAN]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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]
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[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bo/3boy_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bo/3boy_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
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</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=3boy ConSurf].
</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=3boy ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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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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<ref>PMID:15242603</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 3boy" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus globigii migula 1900]]
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[[Category: Bacillus subtilis]]
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[[Category: Balasundaresan, D]]
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[[Category: Large Structures]]
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[[Category: Jeyakanthan, J]]
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[[Category: Balasundaresan D]]
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[[Category: Kumar, P K.R]]
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[[Category: Jeyakanthan J]]
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[[Category: Kumarevel, T S]]
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[[Category: Kumar PKR]]
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[[Category: Structural genomic]]
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[[Category: Kumarevel TS]]
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[[Category: Shinkai, A]]
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[[Category: Shinkai A]]
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[[Category: Yokoyama, S]]
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[[Category: Yokoyama S]]
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[[Category: Activator]]
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[[Category: Anti-termination]]
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[[Category: Histidine metabolism]]
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[[Category: Hutp]]
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[[Category: Hutp-rna complex]]
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[[Category: National project on protein structural and functional analyse]]
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[[Category: Nppsfa]]
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[[Category: Rna-binding]]
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[[Category: Rsgi]]
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[[Category: Transcription regulation]]
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[[Category: Transcription-rna complex]]
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Current revision

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

PDB ID 3boy

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