6q29
From Proteopedia
(Difference between revisions)
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==Crystal structure of Laccase from Thermus thermophilus HB27 with an open conformation of beta-hairpin (Average deposted dose 2.5 MGy)== | ==Crystal structure of Laccase from Thermus thermophilus HB27 with an open conformation of beta-hairpin (Average deposted dose 2.5 MGy)== | ||
| - | <StructureSection load='6q29' size='340' side='right'caption='[[6q29]]' scene=''> | + | <StructureSection load='6q29' size='340' side='right'caption='[[6q29]], [[Resolution|resolution]] 1.70Å' 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=6Q29 OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6q29]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thet2 Thet2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q29 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Q29 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </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=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TT_C1370 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=262724 THET2])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Laccase Laccase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.3.2 1.10.3.2] </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=6q29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q29 OCA], [https://pdbe.org/6q29 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6q29 RCSB], [https://www.ebi.ac.uk/pdbsum/6q29 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6q29 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The multi-copper oxidase from the hyper-thermophilic bacteria Thermus thermophilus (Tth-MCO), has been previously characterized and described as an example of a laccase with low catalytic properties, especially when it is compared with the activity of fungal laccases, but it is active at high temperatures. Structurally, Tth-MCO has a unique feature: a beta-hairpin near the T1Cu site, which is not present in any other laccases deposited at the PDB. This beta-hairpin has an expected crystallographic behavior in solvent-exposed areas of a crystallized protein: lack of electron density, high B-values and several crystalline contacts with neighboring crystallographic copies; however, its dynamical behavior in solution and its biological implications have not been described. Here, we describe four new Tth-MCO crystallographic structures, and the beta-hairpin behavior has been analyzed by molecular dynamics simulations, considering the effect of pH and temperature. The beta-hairpin new crystallographic conformations described here, together with their dynamics, were used to understand the pH-restrained laccase activity of Tth-MCO against substrates as syringaldazine. Remarkably, there are insertions in laccases from Thermus and Meiothermus genus, sharing the same position and a methionine-rich composition of the Tth-MCO beta-hairpin. This unique high methionine content of the Tth-MCO beta-hairpin is responsible to coordinate, Ag(+1) and Hg(+1) in oxidative conditions, but Cu(+1) and Cu(+2) are not coordinated in crystallographic experiments, regardless of the redox conditions; however, Ag(+1) addition does not affect Tth-MCO laccase activity against syringaldazine. Here, we propose that the pH-dependent beta-hairpin dynamical behavior could explain, at least in part, the inefficient laccase activity displayed by Tth-MCO in acidic pH values. | ||
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| + | The beta-hairpin from the Thermus thermophilus HB27 laccase works as a pH-dependent switch to regulate laccase activity.,Miranda-Blancas R, Avelar M, Rodriguez-Arteaga A, Sinicropi A, Rudino-Pinera E J Struct Biol. 2021 Jun;213(2):107740. doi: 10.1016/j.jsb.2021.107740. Epub 2021 , May 5. PMID:33962016<ref>PMID:33962016</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6q29" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Laccase 3D structures|Laccase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Laccase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Miranda-Blancas R]] | + | [[Category: Thet2]] |
| - | [[Category: Rudino-Pinera E]] | + | [[Category: Miranda-Blancas, R]] |
| + | [[Category: Rudino-Pinera, E]] | ||
| + | [[Category: Multicopper oxidase]] | ||
| + | [[Category: Open loop]] | ||
| + | [[Category: Structural protein]] | ||
Revision as of 06:25, 25 August 2021
Crystal structure of Laccase from Thermus thermophilus HB27 with an open conformation of beta-hairpin (Average deposted dose 2.5 MGy)
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