4jhv: Difference between revisions
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<StructureSection load='4jhv' size='340' side='right'caption='[[4jhv]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='4jhv' size='340' side='right'caption='[[4jhv]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4jhv]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4jhv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Coriolopsis_caperata Coriolopsis caperata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JHV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JHV FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PG6:1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-ETHOXY}-ETHANE'>PG6</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PG6:1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-ETHOXY}-ETHANE'>PG6</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4jhv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jhv OCA], [https://pdbe.org/4jhv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jhv RCSB], [https://www.ebi.ac.uk/pdbsum/4jhv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jhv ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/M1GME7_9APHY M1GME7_9APHY] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 4jhv" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4jhv" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Laccase 3D structures|Laccase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Coriolopsis caperata]] | [[Category: Coriolopsis caperata]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Fedorova | [[Category: Fedorova TV]] | ||
[[Category: Glazunova | [[Category: Glazunova OA]] | ||
[[Category: Koroleva | [[Category: Koroleva OV]] | ||
[[Category: Kurzeev | [[Category: Kurzeev SA]] | ||
[[Category: Lamzin | [[Category: Lamzin VS]] | ||
[[Category: Maloshenok | [[Category: Maloshenok LG]] | ||
[[Category: Polyakov | [[Category: Polyakov KM]] | ||
Latest revision as of 06:06, 21 November 2024
T2-depleted laccase from Coriolopsis caperataT2-depleted laccase from Coriolopsis caperata
Structural highlights
FunctionPublication Abstract from PubMedLaccases are members of a large family of multicopper oxidases that catalyze the oxidation of a wide range of organic and inorganic substrates accompanied by the reduction of dioxygen to water. A new laccase was isolated from the basidiomycete Coriolopsis caperata strain 0677 and its amino-acid sequence was determined. According to its physicochemical properties and spectroscopic features, the laccase from C. caperata is a high redox-potential blue laccase. Attempts to crystallize the native enzyme were unsuccessful. The copper type 2-depleted (T2D) laccase was prepared and crystallized. The structure of T2D laccase from C. caperata was solved at 1.6 A resolution, and attempts to reconstruct the T2 copper centre were performed using Cu(+) and Cu(2+) ions. The structure of T2D+Cu(+) laccase was solved at 1.89 A resolution. It was shown that the T2D+Cu(+) laccase structure contained four copper ions in the active site. Reconstruction could not be achieved when the T2D laccase crystals were treated with CuSO4. Elucidation of the crystal structure of Coriolopsis caperata laccase: restoration of the structure and activity of the native enzyme from the T2-depleted form by copper ions.,Glazunova OA, Polyakov KM, Fedorova TV, Dorovatovskii PV, Koroleva OV Acta Crystallogr D Biol Crystallogr. 2015 Apr;71(Pt 4):854-61. doi:, 10.1107/S1399004715001595. Epub 2015 Mar 26. PMID:25849396[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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