5ce9: Difference between revisions
New page: '''Unreleased structure''' The entry 5ce9 is ON HOLD until Paper Publication Authors: Bijelic, A., Pretzler, M., Zekiri, F., Rompel, A. Description: structure of tyrosinase from walnut... |
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==structure of tyrosinase from walnut (Juglans regia)== | |||
<StructureSection load='5ce9' size='340' side='right'caption='[[5ce9]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ce9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Juglans_regia Juglans regia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CE9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CE9 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]] 1.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</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=5ce9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ce9 OCA], [https://pdbe.org/5ce9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ce9 RCSB], [https://www.ebi.ac.uk/pdbsum/5ce9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ce9 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/C0LU17_JUGRE C0LU17_JUGRE] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Tyrosinases and catechol oxidases are members of the class of type III copper enzymes. While tyrosinases accept both mono- and o-diphenols as substrates, only the latter substrate is converted by catechol oxidases. Researchers have been working for decades to elucidate the monophenolase/diphenolase specificity on a structural level and have introduced an early hypothesis that states that the reason for the lack of monophenolase activity in catechol oxidases may be its structurally restricted active site. However, recent structural and biochemical studies of this enzyme class have raised doubts about this theory. Herein, the first crystal structure of a plant tyrosinase (from Juglans regia) is presented. The structure reveals that the distinction between mono- and diphenolase activity does not depend on the degree of restriction of the active site, and thus a more important role for amino acid residues located at the entrance to and in the second shell of the active site is proposed. | |||
The Structure of a Plant Tyrosinase from Walnut Leaves Reveals the Importance of "Substrate-Guiding Residues" for Enzymatic Specificity.,Bijelic A, Pretzler M, Molitor C, Zekiri F, Rompel A Angew Chem Int Ed Engl. 2015 Oct 16. doi: 10.1002/anie.201506994. PMID:26473311<ref>PMID:26473311</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5ce9" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: Zekiri | *[[Tyrosinase 3D structures|Tyrosinase 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Juglans regia]] | |||
[[Category: Large Structures]] | |||
[[Category: Bijelic A]] | |||
[[Category: Pretzler M]] | |||
[[Category: Rompel A]] | |||
[[Category: Zekiri F]] | |||
Latest revision as of 14:19, 10 January 2024
structure of tyrosinase from walnut (Juglans regia)structure of tyrosinase from walnut (Juglans regia)
Structural highlights
FunctionPublication Abstract from PubMedTyrosinases and catechol oxidases are members of the class of type III copper enzymes. While tyrosinases accept both mono- and o-diphenols as substrates, only the latter substrate is converted by catechol oxidases. Researchers have been working for decades to elucidate the monophenolase/diphenolase specificity on a structural level and have introduced an early hypothesis that states that the reason for the lack of monophenolase activity in catechol oxidases may be its structurally restricted active site. However, recent structural and biochemical studies of this enzyme class have raised doubts about this theory. Herein, the first crystal structure of a plant tyrosinase (from Juglans regia) is presented. The structure reveals that the distinction between mono- and diphenolase activity does not depend on the degree of restriction of the active site, and thus a more important role for amino acid residues located at the entrance to and in the second shell of the active site is proposed. The Structure of a Plant Tyrosinase from Walnut Leaves Reveals the Importance of "Substrate-Guiding Residues" for Enzymatic Specificity.,Bijelic A, Pretzler M, Molitor C, Zekiri F, Rompel A Angew Chem Int Ed Engl. 2015 Oct 16. doi: 10.1002/anie.201506994. PMID:26473311[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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