7m1k: Difference between revisions
No edit summary |
No edit summary |
||
| (One intermediate revision by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Crystal structure of dehaloperoxidase B in complex with 2,6-difluorophenol== | ==Crystal structure of dehaloperoxidase B in complex with 2,6-difluorophenol== | ||
<StructureSection load='7m1k' size='340' side='right'caption='[[7m1k]]' scene=''> | <StructureSection load='7m1k' size='340' side='right'caption='[[7m1k]], [[Resolution|resolution]] 1.79Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7M1K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7M1K FirstGlance]. <br> | <table><tr><td colspan='2'>[[7m1k]] 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=7M1K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7M1K FirstGlance]. <br> | ||
</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=7m1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7m1k OCA], [https://pdbe.org/7m1k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7m1k RCSB], [https://www.ebi.ac.uk/pdbsum/7m1k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7m1k ProSAT]</span></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]] 1.795Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FFP:2,6-DIFLUOROPHENOL'>FFP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=7m1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7m1k OCA], [https://pdbe.org/7m1k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7m1k RCSB], [https://www.ebi.ac.uk/pdbsum/7m1k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7m1k ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9NAV7_9ANNE Q9NAV7_9ANNE] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The multifunctional catalytic globin dehaloperoxidase (DHP) from the marine worm Amphitrite ornata was shown to catalyze the H2O2-dependent oxidation of 2,4- and 2,6-dihalophenols (DXP; X = F, Cl, Br). Product identification by LC-MS revealed multiple monomeric products with varying degrees of oxidation and/or dehalogenation, as well as oligomers with n up to 6. Mechanistic and (18)O-labeling studies demonstrated sequential dihalophenol oxidation via peroxidase and peroxygenase activities. Binding studies established that 2,4-DXP (X = Cl, Br) have the highest affinities of any known DHP substrate. X-ray crystallography identified different binding positions for 2,4- and 2,6-DXP substrates in the hydrophobic distal pocket of DHP. Correlation between the number of halogens and the substrate binding orientation revealed a halogen-dependent binding motif for mono- (4-halophenol), di- (2,4- and 2,6-dihalophenol) and trihalophenols (2,4,6-trihalopenol). Taken together, the findings here on dihalophenol reactivity with DHP advance our understanding of how these compounds bridge the inhibitory and oxidative functions of their mono- and trihalophenol counterparts, respectively, and provide further insight into the protein structure-function paradigm relevant to multifunctional catalytic globins in comparison to their monofunctional analogs. | |||
Bridging the functional gap between reactivity and inhibition in dehaloperoxidase B from Amphitrite ornata: Mechanistic and structural studies with 2,4- and 2,6-dihalophenols.,Malewschik T, Carey LM, de Serrano V, Ghiladi RA J Inorg Biochem. 2022 Jul 25;236:111944. doi: 10.1016/j.jinorgbio.2022.111944. PMID:35969974<ref>PMID:35969974</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7m1k" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Dehaloperoxidase 3D structures|Dehaloperoxidase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Amphitrite ornata]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ghiladi RA]] | [[Category: Ghiladi RA]] | ||
[[Category: Malewschik T]] | [[Category: Malewschik T]] | ||
[[Category: De Serrano VS]] | [[Category: De Serrano VS]] | ||