3ta4

<StructureSection load='3ta4' size='340' side='right' caption='[[3ta4]], [[Resolution|resolution]] 2.35&Aring;' scene=''>

<table><tr><td colspan='2'>[[3ta4]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Amycolatopsis_sp._atcc_39116 Amycolatopsis sp. atcc 39116]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TA4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TA4 FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=TO2:(1R,2S)-1-(3,4-DIMETHOXYPHENYL)-2-(2-METHOXYPHENOXY)PROPANE-1,3-DIOL'>TO2</scene><br>

<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3t9w|3t9w]]</td></tr>

<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Laccase Laccase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.3.2 1.10.3.2] </span></td></tr>

<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ta4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ta4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ta4 RCSB], [http://www.ebi.ac.uk/pdbsum/3ta4 PDBsum]</span></td></tr>

<table>

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== Publication Abstract from PubMed ==

Laccases (EC 1.10.3.2) are multicopper oxidases able to oxidize a range of substrates including phenols, aromatic amines and non-phenolic substrates. In order to investigate the involvement of the small Streptomyces laccases in lignin degradation, we generated acid-precipitable polymeric lignin (APPL) obtained in the presence of wild type Streptomyces coelicolor A3(2) (SCWT) and its laccase-less mutant (SCDeltaLAC) in presence of Miscanthus x giganteus lignocellulose. The results showed that strain SCDeltaLAC was inefficient in degrading lignin compared to strain SCWT, thereby supporting the importance of laccase for lignin degradation by Streptomyces coelicolor A3(2). We also studied the lignin degradation activity of laccases from Streptomyces coelicolor A3(2), Streptomyces lividans TK24, Streptomyces viridosporus T7A and Amycolatopsis sp. 75iv2 using both lignin model compounds and ethanosolv lignin. All four laccases degraded a phenolic model compound (LM-OH), but only able to oxidize a non-phenolic model compound (LM-OMe) in the presence of redox mediators. Their activities are highest at pH 8.0 with a low krel/Kapp for LM-OH, suggesting that the enzymes' natural substrates must be different in shape or chemical nature. Crystal structures of the laccases from Streptomyces viridosporus T7A (SVLAC) and Amycolatopsis sp. 75iv2 (AMLAC) were determined both with and without bound substrate. This is the first report of a crystal structure for any laccase bound to a non-phenolic beta-O-4 lignin model compound. An additional zinc metal binding site in SVLAC was also identified. The ability to oxidize/rearrange ethanosolv lignin further provides evidence for the utility of laccase activity for lignin degradation/modification.

 

== References ==

[[Category: Amycolatopsis sp. atcc 39116]]

[[Category: Laccase]]

[[Category: Gerlt, J A.]]

[[Category: Lukk, T.]]

[[Category: Majumdar, S.]]

[[Category: Nair, S K.]]

[[Category: Secreted]]