3eee
From Proteopedia
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| - | + | ==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 [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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EEE FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1u55|1u55]], [[1u56|1u56]], [[1u4h|1u4h]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tar4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=119072 Caldanaerobacter subterraneus subsp. tengcongensis])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3eee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eee OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3eee RCSB], [http://www.ebi.ac.uk/pdbsum/3eee PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == 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/initialview01.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/chain_selection.php?pdb_ID=2ata 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> | ||
==See Also== | ==See Also== | ||
*[[Chemotaxis protein|Chemotaxis protein]] | *[[Chemotaxis protein|Chemotaxis protein]] | ||
*[[Methyl-accepting chemotaxis protein|Methyl-accepting chemotaxis protein]] | *[[Methyl-accepting chemotaxis protein|Methyl-accepting chemotaxis protein]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Caldanaerobacter subterraneus subsp. tengcongensis]] | [[Category: Caldanaerobacter subterraneus subsp. tengcongensis]] | ||
| - | [[Category: Boon, E M | + | [[Category: Boon, E M]] |
| - | [[Category: Jr, C Olea | + | [[Category: Jr, C Olea]] |
| - | [[Category: Kuriyan, J | + | [[Category: Kuriyan, J]] |
| - | [[Category: Marletta, M A | + | [[Category: Marletta, M A]] |
| - | [[Category: Pellicena, P | + | [[Category: Pellicena, P]] |
[[Category: Hemoprotein]] | [[Category: Hemoprotein]] | ||
[[Category: Signaling protein]] | [[Category: Signaling protein]] | ||
Revision as of 14:04, 17 December 2014
Probing the function of heme distortion in the H-NOX family
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