View source for 5g4i


==PLP-dependent phospholyase A1RDF1 from Arthrobacter aurescens TC1==
<StructureSection load='5g4i' size='340' side='right'caption='[[5g4i]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5g4i]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Paenarthrobacter_aurescens_TC1 Paenarthrobacter aurescens TC1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G4I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5G4I 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]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=B3P:2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>B3P</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=5g4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g4i OCA], [https://pdbe.org/5g4i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5g4i RCSB], [https://www.ebi.ac.uk/pdbsum/5g4i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5g4i ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A1RDF1_PAEAT A1RDF1_PAEAT] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
PLP-dependent enzymes catalyze a remarkable diversity of chemical reactions in Nature. A1RDF1 from Arthrobacter aurescens TC1 is a Fold Type I, PLP-dependent enzyme in the Class III transaminase (TA) subgroup. Despite sharing 28% sequence identity with its closest structural homologs, including beta-alanine:pyruvate and gamma-amino butyrate:alpha-ketoglutarate TAs, A1RDF1 displayed no TA activity. Activity screening revealed the enzyme to possess phospholyase (E.C. 4.2.3.2) activity towards O-phosphoethanolamine (PEtN), an activity described previously for vertebrate enzymes such as human AGXT2L1, and for which no structure has yet been reported. In order to shed light on the distinctive features of PLP-dependent phospholyases, structures of A1RDF1 in complex with PLP (internal aldimine) and PLP-PEtN (external aldimine) were determined, revealing the basis of substrate binding and the structural factors that distinguish the enzyme from Class III homologs that display TA activity.

Structural basis for phospholyase activity of a Class III transaminase homolog.,Cuetos A, Steffen-Munsberg F, Mangas Sanchez J, Frese A, Bornscheuer UT, Hohne M, Grogan G Chembiochem. 2016 Oct 6. doi: 10.1002/cbic.201600482. PMID:27709756<ref>PMID:27709756</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5g4i" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Paenarthrobacter aurescens TC1]]
[[Category: Cuetos A]]
[[Category: Grogan G]]
[[Category: Mangas Sanchez J]]
[[Category: Tuan AN]]