4au9: Difference between revisions
From Proteopedia
Jump to navigationJump to search
m Protected "4au9" [edit=sysop:move=sysop] |
No edit summary |
||
| (6 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
The | ==Crystal Structure of a Fungal DyP-Type Peroxidase from Auricularia auricula-judae== | ||
<StructureSection load='4au9' size='340' side='right'caption='[[4au9]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4au9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Auricularia_auricula-judae Auricularia auricula-judae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AU9 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]] 2.1Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</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=4au9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4au9 OCA], [https://pdbe.org/4au9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4au9 RCSB], [https://www.ebi.ac.uk/pdbsum/4au9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4au9 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/DYP_AURAJ DYP_AURAJ] Manganese-independent peroxidase that is able to convert a large number of compounds, but its physiological substrate is not known. In addition to classic peroxidase substrates (e.g. 2,6-dimethoxyphenol), oxidizes dyes such as Reactive Blue 5 and Reactive Black 5.<ref>PMID:19756587</ref> <ref>PMID:23111597</ref> <ref>PMID:25153532</ref> <ref>PMID:25495127</ref> <ref>PMID:25542606</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
DyP-type peroxidases (DyP = dye decolorizing peroxidases) belong to the large group of heme peroxidases. They utilize hydrogen peroxide to catalyze oxidations of various organic compounds. AauDyPI from Auricularia auricula-judae (Fungi) was crystallized and its crystal structure was determined at 2.1 A resolution. The mostly helical structure also shows a beta-sheet motif typical for DyPs and Cld-related structures and includes the complete poypeptide chain. At the distal side of the heme molecule, a flexible aspartate residue (Asp168) plays a key role in catalysis. It guides incoming hydrogen peroxide toward the heme iron and mediates proton rearrangement in the process of Compound I formation. Afterwards, its side chain changes its conformation now pointing toward the protein backbone. We propose an extended functionality of Asp168, that acts like a gatekeeper by altering the width of the heme cavity access channel. Chemical modifications of potentially redox-active amino acids show that a tyrosine is involved in substrate interaction. Using spin trapping experiments a transient radical on the surface-exposed Tyr337 was identified as the oxidation site for bulky substrates. A possible long-range electron transfer (LRET) pathway from the surface of the enzyme to the redox cofactor (heme) is discussed. | |||
First Crystal Structure of a Fungal High-Redox Potential Dye-decolorizing Peroxidase: Substrate Interaction Sites and Long-Range Electron Transfer.,Strittmatter E, Liers C, Ullrich R, Wachter S, Hofrichter M, Plattner DA, Piontek K J Biol Chem. 2012 Dec 12. PMID:23235158<ref>PMID:23235158</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4au9" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Auricularia auricula-judae]] | |||
[[Category: Large Structures]] | |||
[[Category: Hofrichter M]] | |||
[[Category: Liers C]] | |||
[[Category: Pecyna M]] | |||
[[Category: Piontek K]] | |||
[[Category: Plattner DA]] | |||
[[Category: Strittmatter E]] | |||
[[Category: Ullrich R]] | |||
