View source for 4tq3


==Structure of a UbiA homolog from Archaeoglobus fulgidus bound to GPP and Mg2+==
<StructureSection load='4tq3' size='340' side='right'caption='[[4tq3]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4tq3]] 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=4TQ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TQ3 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GPP:GERANYL+DIPHOSPHATE'>GPP</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=4tq3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tq3 OCA], [https://pdbe.org/4tq3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tq3 RCSB], [https://www.ebi.ac.uk/pdbsum/4tq3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tq3 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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4tq3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Archaeoglobus fulgidus DSM 4304]]
[[Category: Large Structures]]
[[Category: Bai Y]]
[[Category: Huang H]]
[[Category: Levin EJ]]
[[Category: Zhou M]]