4it2: Difference between revisions
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==Mn(III)-PPIX bound Tt H-NOX== | |||
<StructureSection load='4it2' size='340' side='right'caption='[[4it2]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4it2]] is a 2 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=4IT2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IT2 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]] 2.097Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MNH:MANGANESE+PROTOPORPHYRIN+IX'>MNH</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=4it2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4it2 OCA], [https://pdbe.org/4it2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4it2 RCSB], [https://www.ebi.ac.uk/pdbsum/4it2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4it2 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8RBX6_CALS4 Q8RBX6_CALS4] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Heme proteins are exquisitely tuned to carry out diverse biological functions while employing identical heme cofactors. Although heme protein properties are often altered through modification of the protein scaffold, protein function can be greatly expanded and diversified through replacement of the native heme with an unnatural porphyrin of interest. Thus, porphyrin substitution in proteins affords new opportunities to rationally tailor heme protein chemical properties for new biological applications. Here, a highly thermally stable Heme Nitric oxide/OXygen binding (H-NOX) protein is evaluated as a magnetic resonance imaging (MRI) contrast agent. T(1) and T(2) relaxivities measured for the H-NOX protein containing its native heme are compared to the protein substituted with unnatural manganese(II/III) and gadolinium(III) porphyrins. H-NOX proteins are found to provide unique porphyrin coordination environments and have enhanced relaxivities compared to commercial small-molecule agents. Porphyrin substitution is a promising strategy to encapsulate MRI-active metals in heme protein scaffolds for future imaging applications. | |||
Porphyrin-Substituted H-NOX Proteins as High-Relaxivity MRI Contrast Agents.,Winter MB, Klemm PJ, Phillips-Piro CM, Raymond KN, Marletta MA Inorg Chem. 2013 Feb 8. PMID:23394479<ref>PMID:23394479</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4it2" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
[[ | *[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Caldanaerobacter subterraneus subsp. tengcongensis]] | [[Category: Caldanaerobacter subterraneus subsp. tengcongensis]] | ||
[[Category: Klemm | [[Category: Large Structures]] | ||
[[Category: Marletta | [[Category: Klemm PJ]] | ||
[[Category: Phillips-Piro | [[Category: Marletta MA]] | ||
[[Category: Raymond | [[Category: Phillips-Piro CM]] | ||
[[Category: Winter | [[Category: Raymond KM]] | ||
[[Category: Winter MB]] | |||
Latest revision as of 18:29, 20 September 2023
Mn(III)-PPIX bound Tt H-NOXMn(III)-PPIX bound Tt H-NOX
Structural highlights
FunctionPublication Abstract from PubMedHeme proteins are exquisitely tuned to carry out diverse biological functions while employing identical heme cofactors. Although heme protein properties are often altered through modification of the protein scaffold, protein function can be greatly expanded and diversified through replacement of the native heme with an unnatural porphyrin of interest. Thus, porphyrin substitution in proteins affords new opportunities to rationally tailor heme protein chemical properties for new biological applications. Here, a highly thermally stable Heme Nitric oxide/OXygen binding (H-NOX) protein is evaluated as a magnetic resonance imaging (MRI) contrast agent. T(1) and T(2) relaxivities measured for the H-NOX protein containing its native heme are compared to the protein substituted with unnatural manganese(II/III) and gadolinium(III) porphyrins. H-NOX proteins are found to provide unique porphyrin coordination environments and have enhanced relaxivities compared to commercial small-molecule agents. Porphyrin substitution is a promising strategy to encapsulate MRI-active metals in heme protein scaffolds for future imaging applications. Porphyrin-Substituted H-NOX Proteins as High-Relaxivity MRI Contrast Agents.,Winter MB, Klemm PJ, Phillips-Piro CM, Raymond KN, Marletta MA Inorg Chem. 2013 Feb 8. PMID:23394479[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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