4fdk
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4fdk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caldanaerobacter_subterraneus_subsp._tengcongensis_MB4 Caldanaerobacter subterraneus subsp. 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 [https://proteopedia.org/fgij/fg.htm?mol=4FDK FirstGlance]. <br> | <table><tr><td colspan='2'>[[4fdk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caldanaerobacter_subterraneus_subsp._tengcongensis_MB4 Caldanaerobacter subterraneus subsp. 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 [https://proteopedia.org/fgij/fg.htm?mol=4FDK FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</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=4fdk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fdk OCA], [https://pdbe.org/4fdk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fdk RCSB], [https://www.ebi.ac.uk/pdbsum/4fdk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fdk ProSAT]</span></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=4fdk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fdk OCA], [https://pdbe.org/4fdk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fdk RCSB], [https://www.ebi.ac.uk/pdbsum/4fdk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fdk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/Q8RBX6_CALS4 Q8RBX6_CALS4] | [https://www.uniprot.org/uniprot/Q8RBX6_CALS4 Q8RBX6_CALS4] | ||
| - | <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. | ||
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| - | 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> | ||
| - | <div class="pdbe-citations 4fdk" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]] | *[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
F78L Tt H-NOX
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