View source for 6klg


==Crystal Structure of the Zea Mays laccase 3==
<StructureSection load='6klg' size='340' side='right'caption='[[6klg]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6klg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KLG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KLG 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]] 2.1&#8491;</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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</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=6klg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6klg OCA], [https://pdbe.org/6klg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6klg RCSB], [https://www.ebi.ac.uk/pdbsum/6klg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6klg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q2PAJ1_MAIZE Q2PAJ1_MAIZE] Lignin degradation and detoxification of lignin-derived products.[RuleBase:RU361119]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Plant laccases catalyse the oxidation of monolignols in lignification, a process reinforcing the cell wall of many different cell types that provide mechanical support, nutrient transportation and defence against pathogens in plants(1). The isozymes display a broad range of substrate preferences. Here, the substrate preference of a laccase (ZmLac3) from Zea mays (maize) was characterized. The crystal structure of ZmLac3 revealed a compact and deep substrate-binding pocket, and the binding modes of sinapyl alcohol (SinA) and coniferyl alcohol (ConA) were solved. On the basis of structural data and kinetics analysis, we propose that the regionalization of polar and hydrophobic surfaces in the binding pocket of ZmLac3 is vital for defining the orientation of SinA/ConA binding. The extra methoxyl group in SinA makes substantial contributions to interactions between SinA and ZmLac3, which are absent in the ZmLac3-ConA complex. In summary, the polar and hydrophobic interactions between SinA/ConA and ZmLac3 determine the binding positions of the monolignols in ZmLac3. These results provide valuable insight about ZmLac3 catalysis and should aid industrial processes that use plant laccases.

Structural basis for monolignol oxidation by a maize laccase.,Xie T, Liu Z, Wang G Nat Plants. 2020 Mar 2. pii: 10.1038/s41477-020-0595-5. doi:, 10.1038/s41477-020-0595-5. PMID:32123349<ref>PMID:32123349</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6klg" style="background-color:#fffaf0;"></div>

==See Also==
*[[Laccase 3D structures|Laccase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Zea mays]]
[[Category: Liu ZC]]
[[Category: Wang GG]]
[[Category: Xie T]]