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==Structure of a UbiA homolog from Archaeoglobus fulgidus== | ==Structure of a UbiA homolog from Archaeoglobus fulgidus== | ||
<StructureSection load='4tq5' size='340' side='right' caption='[[4tq5]], [[Resolution|resolution]] 3.20Å' scene=''> | <StructureSection load='4tq5' size='340' side='right'caption='[[4tq5]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4tq5]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TQ5 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4tq5]] is a 1 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=4TQ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TQ5 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2023Å</td></tr> | ||
<tr><td class="sblockLbl"><b>[[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4tq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tq5 OCA], [https://pdbe.org/4tq5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tq5 RCSB], [https://www.ebi.ac.uk/pdbsum/4tq5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tq5 ProSAT]</span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </table> | ||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4tq5" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Archaeoglobus fulgidus DSM 4304]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Bai Y]] | ||
[[Category: | [[Category: Huang H]] | ||
[[Category: | [[Category: Levin EJ]] | ||
[[Category: | [[Category: Zhou M]] | ||
Latest revision as of 03:47, 28 December 2023
Structure of a UbiA homolog from Archaeoglobus fulgidusStructure of a UbiA homolog from Archaeoglobus fulgidus
Structural highlights
FunctionPublication Abstract from PubMedMembrane-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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