View source for 4fdk


==F78L Tt H-NOX==
<StructureSection load='4fdk' size='340' side='right' caption='[[4fdk]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4fdk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cals4 Cals4]. 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 CALS4])</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://pdbe.org/4fdk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fdk RCSB], [http://www.ebi.ac.uk/pdbsum/4fdk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fdk ProSAT]</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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4fdk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Cals4]]
[[Category: Marletta, M A]]
[[Category: Phillips-Piro, C M]]
[[Category: Weinert, E E]]
[[Category: O2-sensor]]
[[Category: Signaling protein]]