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1wpv

From Proteopedia

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[[Image:1wpv.gif|left|200px]]
 
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{{Structure
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==Crystal Structure of Activated Binary complex of HutP, an RNA binding anti-termination protein==
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|PDB= 1wpv |SIZE=350|CAPTION= <scene name='initialview01'>1wpv</scene>, resolution 1.70&Aring;
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<StructureSection load='1wpv' size='340' side='right'caption='[[1wpv]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=HIS:HISTIDINE'>HIS</scene>
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<table><tr><td colspan='2'>[[1wpv]] is a 3 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=1WPV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WPV FirstGlance]. <br>
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|ACTIVITY=
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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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|GENE=
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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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}}
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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=1wpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wpv OCA], [https://pdbe.org/1wpv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wpv RCSB], [https://www.ebi.ac.uk/pdbsum/1wpv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wpv ProSAT]</span></td></tr>
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</table>
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'''Crystal Structure of Activated Binary complex of HutP, an RNA binding anti-termination protein'''
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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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==Overview==
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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/wp/1wpv_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=1wpv 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 ==
HutP regulates the expression of the hut structural genes of Bacillus subtilis by an anti-termination mechanism and requires two components, Mg2+ ions and L-histidine. HutP recognizes three UAG triplet units, separated by four non-conserved nucleotides on the terminator region. Here we report the 1.60-A resolution crystal structure of the quaternary complex (HutP-L-histidine-Mg2+-21-base single-stranded RNA). In the complex, the RNA adopts a novel triangular fold on the hexameric surface of HutP, without any base-pairing, and binds to the protein mostly by specific protein-base interactions. The structure explains how the HutP and RNA interactions are regulated critically by the l-histidine and Mg2+ ion through the structural rearrangement. To gain insights into these structural rearrangements, we solved two additional crystal structures (uncomplexed HutP and HutP-L-histidine-Mg2+) that revealed the intermediate structures of HutP (before forming an active structure) and the importance of the Mg2+ ion interactions in the complexes.
HutP regulates the expression of the hut structural genes of Bacillus subtilis by an anti-termination mechanism and requires two components, Mg2+ ions and L-histidine. HutP recognizes three UAG triplet units, separated by four non-conserved nucleotides on the terminator region. Here we report the 1.60-A resolution crystal structure of the quaternary complex (HutP-L-histidine-Mg2+-21-base single-stranded RNA). In the complex, the RNA adopts a novel triangular fold on the hexameric surface of HutP, without any base-pairing, and binds to the protein mostly by specific protein-base interactions. The structure explains how the HutP and RNA interactions are regulated critically by the l-histidine and Mg2+ ion through the structural rearrangement. To gain insights into these structural rearrangements, we solved two additional crystal structures (uncomplexed HutP and HutP-L-histidine-Mg2+) that revealed the intermediate structures of HutP (before forming an active structure) and the importance of the Mg2+ ion interactions in the complexes.
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==About this Structure==
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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:15758992<ref>PMID:15758992</ref>
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1WPV 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=1WPV 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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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]
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</div>
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<div class="pdbe-citations 1wpv" 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: 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: HIS]]
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[[Category: MG]]
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[[Category: allosteric activation]]
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[[Category: antitermination]]
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[[Category: conformational change]]
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[[Category: hutp]]
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[[Category: l-histidine]]
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[[Category: rna binding]]
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[[Category: transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:00:06 2008''
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Current revision

Crystal Structure of Activated Binary complex of HutP, an RNA binding anti-termination protein

PDB ID 1wpv

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