This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
6tyr
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==Crystal structure of Laccase from Thermus thermophilus HB27 with a close conformation of its beta-hairpin== | ==Crystal structure of Laccase from Thermus thermophilus HB27 with a close conformation of its beta-hairpin== | ||
| - | <StructureSection load='6tyr' size='340' side='right'caption='[[6tyr]]' scene=''> | + | <StructureSection load='6tyr' size='340' side='right'caption='[[6tyr]], [[Resolution|resolution]] 1.81Å' 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=6TYR OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6tyr]] 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=6TYR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TYR 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=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=6tyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tyr OCA], [https://pdbe.org/6tyr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tyr RCSB], [https://www.ebi.ac.uk/pdbsum/6tyr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tyr 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. | ||
| + | |||
| + | 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> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6tyr" 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: Close loop]] | ||
| + | [[Category: Multicopper oxidase]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 06:25, 25 August 2021
Crystal structure of Laccase from Thermus thermophilus HB27 with a close conformation of its beta-hairpin
| |||||||||||
