6liu: Difference between revisions

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<StructureSection load='6liu' size='340' side='right'caption='[[6liu]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='6liu' size='340' side='right'caption='[[6liu]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6liu]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LIU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6LIU FirstGlance]. <br>
<table><tr><td colspan='2'>[[6liu]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Papaver_somniferum Papaver somniferum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LIU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LIU FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6liu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6liu OCA], [http://pdbe.org/6liu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6liu RCSB], [http://www.ebi.ac.uk/pdbsum/6liu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6liu ProSAT]</span></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]] 2.8&#8491;</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=6liu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6liu OCA], [https://pdbe.org/6liu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6liu RCSB], [https://www.ebi.ac.uk/pdbsum/6liu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6liu ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/TYDC2_PAPSO TYDC2_PAPSO]] Marginally higher substrate specificity for L-DOPA over L-tyrosine.
[https://www.uniprot.org/uniprot/TYDC2_PAPSO TYDC2_PAPSO] Marginally higher substrate specificity for L-DOPA over L-tyrosine.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Plant tyrosine decarboxylase (TyrDC) is a group II pyridoxal 5'-phosphate (PLP)-dependent decarboxylase that mainly catalyzes the decarboxylation of tyrosine to tyramine. This is biologically important for diverting essential primary metabolites into secondary metabolic pathways. Intensive studies have characterized the effective of PLP-binding and the substrate specificity of mammalian 3,4-dihydroxyphenyl-l-alanine (Dopa) decarboxylases, a member of group II PLP-dependent decarboxylase. However, the characteristics of PLP binding and substrate specificity of plant TyrDCs remain unknown. In this study, we focus on the PLP binding manner, and determined the crystal structures of the apo and PLP binding form of type II TyrDC from Papaver somniferum (PsTyrDCII and PsTyrDCII-PLP). The structures showed that, unlike mammalian Dopa decarboxylase, the binding of PLP does not induce distinct conformational changes of PsTyrDCII regarding the overall structure, but the PLP binding pocket displays conformational changes at Phe124, His203 and Thr262. Combining structural comparation and the obtained biochemical findings, it is demonstrated that PsTyrDCII does not binds PLP tightly. Such characteristics of PLP binding may be required by its catalytic reaction and substrate binding. The activity of TyrDC probably regulated by the concentration of PLP in cells.


Crystal structures clarify cofactor binding of plant tyrosine decarboxylase.,Wang H, Yu J, Satoh Y, Nakagawa Y, Tanaka R, Kato K, Yao M Biochem Biophys Res Commun. 2020 Mar 5;523(2):500-505. doi:, 10.1016/j.bbrc.2019.12.077. Epub 2019 Dec 30. PMID:31898973<ref>PMID:31898973</ref>
==See Also==
 
*[[DOPA decarboxylase|DOPA decarboxylase]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6liu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Wang, H]]
[[Category: Papaver somniferum]]
[[Category: Yao, M]]
[[Category: Wang H]]
[[Category: Yu, J]]
[[Category: Yao M]]
[[Category: Apo form]]
[[Category: Yu J]]
[[Category: Decarboxylase]]
[[Category: Lyase]]
[[Category: Plp binding]]
[[Category: Tyrosine]]

Latest revision as of 10:35, 1 May 2024

Crystal structure of apo Tyrosine decarboxylaseCrystal structure of apo Tyrosine decarboxylase

Structural highlights

6liu is a 6 chain structure with sequence from Papaver somniferum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TYDC2_PAPSO Marginally higher substrate specificity for L-DOPA over L-tyrosine.

See Also

6liu, resolution 2.80Å

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