|
|
| Line 3: |
Line 3: |
| | <StructureSection load='6q29' size='340' side='right'caption='[[6q29]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='6q29' size='340' side='right'caption='[[6q29]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <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> | + | <table><tr><td colspan='2'>[[6q29]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB27 Thermus thermophilus HB27]. 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='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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.702Å</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='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='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> | | <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> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q72HW2_THET2 Q72HW2_THET2] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 25: |
Line 26: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Laccase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thet2]] | + | [[Category: Thermus thermophilus HB27]] |
| - | [[Category: Miranda-Blancas, R]] | + | [[Category: Miranda-Blancas R]] |
| - | [[Category: Rudino-Pinera, E]] | + | [[Category: Rudino-Pinera E]] |
| - | [[Category: Multicopper oxidase]]
| + | |
| - | [[Category: Open loop]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
Q72HW2_THET2
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Miranda-Blancas R, Avelar M, Rodriguez-Arteaga A, Sinicropi A, Rudino-Pinera E. The beta-hairpin from the Thermus thermophilus HB27 laccase works as a pH-dependent switch to regulate laccase activity. J Struct Biol. 2021 Jun;213(2):107740. doi: 10.1016/j.jsb.2021.107740. Epub 2021 , May 5. PMID:33962016 doi:http://dx.doi.org/10.1016/j.jsb.2021.107740
|
