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[[Image:3eee.png|left|200px]]


{{STRUCTURE_3eee| PDB=3eee | SCENE= }}
==Probing the function of heme distortion in the H-NOX family==
<StructureSection load='3eee' size='340' side='right'caption='[[3eee]], [[Resolution|resolution]] 2.12&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3eee]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Caldanaerobacter_subterraneus_subsp._tengcongensis Caldanaerobacter subterraneus subsp. tengcongensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EEE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EEE 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]] 2.12&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3eee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eee OCA], [https://pdbe.org/3eee PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eee RCSB], [https://www.ebi.ac.uk/pdbsum/3eee PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eee ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8RBX6_CALS4 Q8RBX6_CALS4]
== 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/ee/3eee_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=3eee ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Hemoproteins carry out diverse functions utilizing a wide range of chemical reactivity while employing the same heme prosthetic group. It is clear from high-resolution crystal structures and biochemical studies that protein-bound hemes are not planar and adopt diverse conformations. The crystal structure of an H-NOX domain from Thermoanaerobacter tengcongensis (Tt H-NOX) contains the most distorted heme reported to date. In this study, Tt H-NOX was engineered to adopt a flatter heme by mutating proline 115, a conserved residue in the H-NOX family, to alanine. Decreasing heme distortion in Tt H-NOX increases affinity for oxygen and decreases the reduction potential of the heme iron. Additionally, flattening the heme is associated with significant shifts in the N-terminus of the protein. These results show a clear link between the heme conformation and Tt H-NOX structure and demonstrate that heme distortion is an important determinant for maintaining biochemical properties in H-NOX proteins.


===Probing the function of heme distortion in the H-NOX family===
Probing the function of heme distortion in the H-NOX family.,Olea C, Boon EM, Pellicena P, Kuriyan J, Marletta MA ACS Chem Biol. 2008 Nov 21;3(11):703-10. PMID:19032091<ref>PMID:19032091</ref>


{{ABSTRACT_PUBMED_19032091}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 3eee" style="background-color:#fffaf0;"></div>
[[3eee]] is a 4 chain structure of [[Methyl-accepting chemotaxis protein]] with sequence from [http://en.wikipedia.org/wiki/Caldanaerobacter_subterraneus_subsp._tengcongensis Caldanaerobacter subterraneus subsp. tengcongensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EEE OCA].


==See Also==
==See Also==
*[[Chemotaxis protein|Chemotaxis protein]]
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
*[[Methyl-accepting chemotaxis protein|Methyl-accepting chemotaxis protein]]
*[[Methyl-accepting chemotaxis protein|Methyl-accepting chemotaxis protein]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:019032091</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Caldanaerobacter subterraneus subsp. tengcongensis]]
[[Category: Caldanaerobacter subterraneus subsp. tengcongensis]]
[[Category: Boon, E M.]]
[[Category: Large Structures]]
[[Category: Jr, C Olea.]]
[[Category: Boon EM]]
[[Category: Kuriyan, J.]]
[[Category: Kuriyan J]]
[[Category: Marletta, M A.]]
[[Category: Marletta MA]]
[[Category: Pellicena, P.]]
[[Category: Olea Jr C]]
[[Category: Hemoprotein]]
[[Category: Pellicena P]]
[[Category: Signaling protein]]
Retrieved from "https://proteopedia.org/3eee"