1vea

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(New page: 200px<br /><applet load="1vea" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vea, resolution 2.80&Aring;" /> '''Crystal Structure of...)
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[[Image:1vea.jpg|left|200px]]<br /><applet load="1vea" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1vea, resolution 2.80&Aring;" />
 
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'''Crystal Structure of HutP, an RNA binding antitermination protein'''<br />
 
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==Overview==
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==Crystal Structure of HutP, an RNA binding antitermination protein==
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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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<StructureSection load='1vea' size='340' side='right'caption='[[1vea]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1vea]] is a 2 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=1VEA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VEA FirstGlance]. <br>
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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]] 2.8&#8491;</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=HBN:N-(2-NAPHTHYL)HISTIDINAMIDE'>HBN</scene></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=1vea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vea OCA], [https://pdbe.org/1vea PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vea RCSB], [https://www.ebi.ac.uk/pdbsum/1vea PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vea ProSAT]</span></td></tr>
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</table>
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== Function ==
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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]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ve/1vea_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1vea ConSurf].
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<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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==About this Structure==
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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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1VEA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with HBN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VEA OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15242603 15242603]
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</div>
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<div class="pdbe-citations 1vea" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Fujimoto, Z.]]
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[[Category: Fujimoto Z]]
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[[Category: Karthe, P.]]
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[[Category: Karthe P]]
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[[Category: Kumar, P.K.R.]]
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[[Category: Kumar PKR]]
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[[Category: Kumarevel, T.S.]]
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[[Category: Kumarevel TS]]
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[[Category: Mizuno, H.]]
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[[Category: Mizuno H]]
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[[Category: Oda, M.]]
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[[Category: Oda M]]
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[[Category: HBN]]
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[[Category: antiterminator]]
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[[Category: hutp]]
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[[Category: regulation of transcription]]
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[[Category: rna binding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:46:17 2007''
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Current revision

Crystal Structure of HutP, an RNA binding antitermination protein

PDB ID 1vea

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