7y8c: Difference between revisions
m Protected "7y8c" [edit=sysop:move=sysop] |
No edit summary |
||
| (2 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Crystal structure of CotA laccase complexed with syringaldehyde== | |||
<StructureSection load='7y8c' size='340' side='right'caption='[[7y8c]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7y8c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Y8C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Y8C 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]] 2Å</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=IJV:3,5-dimethoxy-4-oxidanyl-benzaldehyde'>IJV</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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=7y8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7y8c OCA], [https://pdbe.org/7y8c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7y8c RCSB], [https://www.ebi.ac.uk/pdbsum/7y8c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7y8c ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/COTA_BACSU COTA_BACSU] Involved in brown pigmentation during sporogenesis. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
CotA laccases are multicopper oxidases known for promiscuously oxidizing a broad range of substrates. However, studying substrate promiscuity is limited by the complexity of electron transfer (ET) between substrates and laccases. Here, a systematic analysis of factors affecting ET including electron donor acceptor coupling (Eta(DA)), driving force (DeltaG) and reorganization energy (lambda) was done. Catalysis rates of syringic acid (SA), syringaldehyde (SAD) and acetosyringone (AS) (kcat(SAD) > kcat(SA) > kcat(AS)) are not entirely dependent on the ability to form phenol radicals indicated by DeltaG and lambda calculated by Density Functional Theory (SA < SAD approximately AS). In determined CotA/SA and CotA/SAD structures, SA and SAD bound at 3.9 and 3.7 A away from T1 Cu coordinating His419 ensuring a similar Eta(DA). Abilities of substrate to form phenol radicals could mainly account for difference between kcat(SAD) and kcat(SA). Furthermore, substrate pocket is solvent exposed at the para site of substrate's phenol hydroxyl, which would destabilize binding of AS in the same orientation and position resulting in low kcat. Our results indicated shallow partially covered binding site with propensity of amino acids distribution might help CotA discriminate lignin-phenol derivatives. These findings give new insights for developing specific catalysts for industrial application. | |||
Molecular insights into substrate promiscuity of CotA laccase catalyzing lignin-phenol derivatives.,Li J, Liu Z, Zhao J, Wang G, Xie T Int J Biol Macromol. 2024 Jan;256(Pt 2):128487. doi: , 10.1016/j.ijbiomac.2023.128487. Epub 2023 Dec 1. PMID:38042324<ref>PMID:38042324</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7y8c" style="background-color:#fffaf0;"></div> | ||
[[Category: Wang | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus subtilis subsp. subtilis str. 168]] | |||
[[Category: Large Structures]] | |||
[[Category: Liu ZC]] | |||
[[Category: Wang GG]] | |||
[[Category: Xie T]] | |||
Latest revision as of 12:42, 9 October 2024
Crystal structure of CotA laccase complexed with syringaldehydeCrystal structure of CotA laccase complexed with syringaldehyde
Structural highlights
FunctionCOTA_BACSU Involved in brown pigmentation during sporogenesis. Publication Abstract from PubMedCotA laccases are multicopper oxidases known for promiscuously oxidizing a broad range of substrates. However, studying substrate promiscuity is limited by the complexity of electron transfer (ET) between substrates and laccases. Here, a systematic analysis of factors affecting ET including electron donor acceptor coupling (Eta(DA)), driving force (DeltaG) and reorganization energy (lambda) was done. Catalysis rates of syringic acid (SA), syringaldehyde (SAD) and acetosyringone (AS) (kcat(SAD) > kcat(SA) > kcat(AS)) are not entirely dependent on the ability to form phenol radicals indicated by DeltaG and lambda calculated by Density Functional Theory (SA < SAD approximately AS). In determined CotA/SA and CotA/SAD structures, SA and SAD bound at 3.9 and 3.7 A away from T1 Cu coordinating His419 ensuring a similar Eta(DA). Abilities of substrate to form phenol radicals could mainly account for difference between kcat(SAD) and kcat(SA). Furthermore, substrate pocket is solvent exposed at the para site of substrate's phenol hydroxyl, which would destabilize binding of AS in the same orientation and position resulting in low kcat. Our results indicated shallow partially covered binding site with propensity of amino acids distribution might help CotA discriminate lignin-phenol derivatives. These findings give new insights for developing specific catalysts for industrial application. Molecular insights into substrate promiscuity of CotA laccase catalyzing lignin-phenol derivatives.,Li J, Liu Z, Zhao J, Wang G, Xie T Int J Biol Macromol. 2024 Jan;256(Pt 2):128487. doi: , 10.1016/j.ijbiomac.2023.128487. Epub 2023 Dec 1. PMID:38042324[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||