4tq4: Difference between revisions

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-'''Unreleased structure'''
-The entry 4tq4 is ON HOLD
+==Structure of a UbiA homolog from Archaeoglobus fulgidus bound to DMAPP and Mg2+==
+<StructureSection load='4tq4' size='340' side='right'caption='[[4tq4]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4tq4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus_DSM_4304 Archaeoglobus fulgidus DSM 4304]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TQ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TQ4 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]] 2.5025&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMA:DIMETHYLALLYL+DIPHOSPHATE'>DMA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4tq4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tq4 OCA], [https://pdbe.org/4tq4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tq4 RCSB], [https://www.ebi.ac.uk/pdbsum/4tq4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tq4 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/O28625_ARCFU O28625_ARCFU]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Membrane-embedded prenyltransferases from the UbiA family catalyze the Mg2+-dependent transfer of a hydrophobic polyprenyl chain onto a variety of acceptor molecules and are involved in the synthesis of molecules that mediate electron transport, including Vitamin K and Coenzyme Q. In humans, missense mutations to the protein UbiA prenyltransferase domain-containing 1 (UBIAD1) are responsible for Schnyder crystalline corneal dystrophy, which is a genetic disease that causes blindness. Mechanistic understanding of this family of enzymes has been hampered by a lack of three-dimensional structures. We have solved structures of a UBIAD1 homolog from Archaeoglobus fulgidus, AfUbiA, in an unliganded form and bound to Mg2+ and two different isoprenyl diphosphates. Functional assays on MenA, a UbiA family member from E. coli, verified the importance of residues involved in Mg2+ and substrate binding. The structural and functional studies led us to propose a mechanism for the prenyl transfer reaction. Disease-causing mutations in UBIAD1 are clustered around the active site in AfUbiA, suggesting the mechanism of catalysis is conserved between the two homologs.
-Authors: Huang, H., Levin, E.J., Bai, Y., Zhou, M., New York Consortium on Membrane Protein Structure (NYCOMPS)
+Structure of a Membrane-Embedded Prenyltransferase Homologous to UBIAD1.,Huang H, Levin EJ, Liu S, Bai Y, Lockless SW, Zhou M PLoS Biol. 2014 Jul 22;12(7):e1001911. doi: 10.1371/journal.pbio.1001911., eCollection 2014 Jul. PMID:25051182<ref>PMID:25051182</ref>
-Description: Structure of a UbiA homolog from Archaeoglobus fulgidus bound to DMAPP and Mg2+
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4tq4" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Archaeoglobus fulgidus DSM 4304]]
+[[Category: Large Structures]]
+[[Category: Bai Y]]
+[[Category: Huang H]]
+[[Category: Levin EJ]]
+[[Category: Zhou M]]