4fdk
From Proteopedia
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| - | + | ==F78L Tt H-NOX== | |
| - | === | + | <StructureSection load='4fdk' size='340' side='right' caption='[[4fdk]], [[Resolution|resolution]] 2.10Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4fdk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermoanaerobacter_tengcongensis_mb4 Thermoanaerobacter tengcongensis mb4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FDK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FDK FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1u55|1u55]], [[1u4h|1u4h]], [[1u56|1u56]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tar4, TTE0680 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273068 Thermoanaerobacter tengcongensis MB4])</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=4fdk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fdk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fdk RCSB], [http://www.ebi.ac.uk/pdbsum/4fdk PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The role of pi-stacking in controlling redox and ligand binding properties of porphyrins has been of interest for many years. The recent discovery of H-NOX domains has provided a model system to investigate the role of porphyrin pi-stacking within a heme protein scaffold. Removal of a phenylalanine-porphyrin pi-stack dramatically increased O2, NO, and CO affinities and caused changes in redox potential (~40mV) without any structural changes. These results suggest that small changes in redox potential affect ligand affinity and that pi-stacking may provide a novel route to engineer heme protein properties for new functions. | ||
| - | + | Porphyrin pi-stacking in a heme protein scaffold tunes gas ligand affinity.,Weinert EE, Phillips-Piro CM, Marletta MA J Inorg Biochem. 2013 Jun 15;127C:7-12. doi: 10.1016/j.jinorgbio.2013.06.004. PMID:23831583<ref>PMID:23831583</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | |||
| + | ==See Also== | ||
| + | *[[Chemotaxis protein|Chemotaxis protein]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Thermoanaerobacter tengcongensis mb4]] | [[Category: Thermoanaerobacter tengcongensis mb4]] | ||
| - | [[Category: Marletta, M A | + | [[Category: Marletta, M A]] |
| - | [[Category: Phillips-Piro, C M | + | [[Category: Phillips-Piro, C M]] |
| - | [[Category: Weinert, E E | + | [[Category: Weinert, E E]] |
[[Category: O2-sensor]] | [[Category: O2-sensor]] | ||
[[Category: Signaling protein]] | [[Category: Signaling protein]] | ||
Revision as of 11:14, 21 December 2014
F78L Tt H-NOX
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