3eee: Difference between revisions
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New page: '''Unreleased structure''' The entry 3eee is ON HOLD Authors: Olea Jr, Charles, Boon, Elizabeth M., Pellicena, Patricia, Kuriyan, John, Marletta, Michael A. Description: Probing the fu... |
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The | ==Probing the function of heme distortion in the H-NOX family== | ||
<StructureSection load='3eee' size='340' side='right'caption='[[3eee]], [[Resolution|resolution]] 2.12Å' 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]] 2.12Å</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.,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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3eee" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]] | |||
*[[Methyl-accepting chemotaxis protein|Methyl-accepting chemotaxis protein]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Caldanaerobacter subterraneus subsp. tengcongensis]] | |||
[[Category: Large Structures]] | |||
[[Category: Boon EM]] | |||
[[Category: Kuriyan J]] | |||
[[Category: Marletta MA]] | |||
[[Category: Olea Jr C]] | |||
[[Category: Pellicena P]] | |||
