4jac: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4jac]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Amphitrite_ornata Amphitrite ornata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JAC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JAC FirstGlance]. <br>
<table><tr><td colspan='2'>[[4jac]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Amphitrite_ornata Amphitrite ornata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JAC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JAC FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.934&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4jac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jac OCA], [https://pdbe.org/4jac PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jac RCSB], [https://www.ebi.ac.uk/pdbsum/4jac PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jac 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=4jac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jac OCA], [https://pdbe.org/4jac PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jac RCSB], [https://www.ebi.ac.uk/pdbsum/4jac PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jac ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/Q9NAV8_9ANNE Q9NAV8_9ANNE]  
[https://www.uniprot.org/uniprot/Q9NAV8_9ANNE Q9NAV8_9ANNE]  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The activation of dehaloperoxidase-hemoglobin (DHP) to form a ferryl intermediate requires the distal histidine, H55, to act as an acid base catalyst. The lack of ancillary amino acids in the distal pocket to assist in this process makes H55 even more important to the formation of active intermediates than in conventional peroxidases. Therefore, one can infer that the precise conformation H55 may greatly affect the enzymatic activity. Using site-direct mutagenesis at position T56, immediately adjacent to H55, we have confirmed that subtle changes in the conformation of H55 affect the catalytic efficiency of DHP. Mutating T56 to a smaller amino acid appears to permit H55 to rotate with relatively low barriers between conformations in the distal pocket, which may lead to an increase in catalytic activity. On the other hand, larger amino acids in the neighboring site appear to restrict the rotation of H55 due to the steric hindrance. In the case of T56V, which is an isosteric mutation, H55 appears less mobile, but forced to be closer to the heme iron than in wild type. Both proximity to the heme iron and flexibility of motion in some of the mutants can result in an increased catalytic rate, but can also lead to protein inactivation due to ligation of H55 to the heme iron, which is known as hemichrome formation. A balance of enzymatic rate and protein stability with respect to hemichrome formation appears to be optimum in wild type DHP (WT-DHP).
The role of T56 in controlling the flexibility of the distal histidine in dehaloperoxidase-hemoglobin from Amphitrite ornata.,Jiang S, Wright I, Swartz P, Franzen S Biochim Biophys Acta. 2013 Oct;1834(10):2020-9. doi:, 10.1016/j.bbapap.2013.06.005. Epub 2013 Jun 20. PMID:23792762<ref>PMID:23792762</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4jac" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Dehaloperoxidase 3D structures|Dehaloperoxidase 3D structures]]
*[[Dehaloperoxidase 3D structures|Dehaloperoxidase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Latest revision as of 15:02, 1 March 2024

Dehaloperoxidase-Hemoglobin T56SDehaloperoxidase-Hemoglobin T56S

Structural highlights

4jac is a 2 chain structure with sequence from Amphitrite ornata. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.934Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9NAV8_9ANNE

See Also

4jac, resolution 1.93Å

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