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New page: left|200px<br /><applet load="1or4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1or4, resolution 2.15Å" /> '''Crystal Structure of...
 
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[[Image:1or4.gif|left|200px]]<br /><applet load="1or4" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1or4, resolution 2.15&Aring;" />
'''Crystal Structure of HemAT sensor domain from B.subtilis in the cyano-liganded form'''<br />


==Overview==
==Crystal Structure of HemAT sensor domain from B.subtilis in the cyano-liganded form==
Much is now known about chemotaxis signaling transduction for Escherichia, coli and Salmonella typhimurium. The mechanism of chemotaxis of Bacillus, subtilis is, in a sense, reversed. Attractant binding strengthens the, activity of histidine kinase in B. subtilis, instead of an inhibition, reaction. The HemAT from B. subtilis can detect oxygen and transmit the, signal to regulatory proteins that control the direction of flagella, rotation. We have determined the crystal structures of the HemAT sensor, domain in liganded and unliganded forms at 2.15 A and 2.7 A resolution, respectively. The liganded structure reveals a highly symmetrical, organization. Tyrosine70 shows distinct conformational changes on one, subunit when ligands are removed. Our study suggests that disruption of, the symmetry of HemAT plays an important role in initiating the chemotaxis, signaling transduction cascade.
<StructureSection load='1or4' size='340' side='right'caption='[[1or4]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1or4]] 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=1OR4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OR4 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1or4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1or4 OCA], [https://pdbe.org/1or4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1or4 RCSB], [https://www.ebi.ac.uk/pdbsum/1or4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1or4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HEMAT_BACSU HEMAT_BACSU] Heme-containing signal transducer responsible for aerotaxis, the migratory response toward or away from oxygen.<ref>PMID:10676961</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/or/1or4_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1or4 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Much is now known about chemotaxis signaling transduction for Escherichia coli and Salmonella typhimurium. The mechanism of chemotaxis of Bacillus subtilis is, in a sense, reversed. Attractant binding strengthens the activity of histidine kinase in B. subtilis, instead of an inhibition reaction. The HemAT from B. subtilis can detect oxygen and transmit the signal to regulatory proteins that control the direction of flagella rotation. We have determined the crystal structures of the HemAT sensor domain in liganded and unliganded forms at 2.15 A and 2.7 A resolution, respectively. The liganded structure reveals a highly symmetrical organization. Tyrosine70 shows distinct conformational changes on one subunit when ligands are removed. Our study suggests that disruption of the symmetry of HemAT plays an important role in initiating the chemotaxis signaling transduction cascade.


==About this Structure==
Structure of the oxygen sensor in Bacillus subtilis: signal transduction of chemotaxis by control of symmetry.,Zhang W, Phillips GN Jr Structure. 2003 Sep;11(9):1097-110. PMID:12962628<ref>PMID:12962628</ref>
1OR4 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 CYN and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OR4 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structure of the oxygen sensor in Bacillus subtilis: signal transduction of chemotaxis by control of symmetry., Zhang W, Phillips GN Jr, Structure. 2003 Sep;11(9):1097-110. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12962628 12962628]
</div>
<div class="pdbe-citations 1or4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Jr., G.N.Phillips.]]
[[Category: Phillips Jr GN]]
[[Category: Zhang, W.]]
[[Category: Zhang W]]
[[Category: CYN]]
[[Category: HEM]]
[[Category: globin fold]]
 
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