4tq6: Difference between revisions
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==Structure of a UbiA homolog from Archaeoglobus fulgidus bound to Cd2+== | ==Structure of a UbiA homolog from Archaeoglobus fulgidus bound to Cd2+== | ||
<StructureSection load='4tq6' size='340' side='right' caption='[[4tq6]], [[Resolution|resolution]] 3.07Å' scene=''> | <StructureSection load='4tq6' size='340' side='right'caption='[[4tq6]], [[Resolution|resolution]] 3.07Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4tq6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfu Arcfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TQ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TQ6 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4tq6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfu Arcfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TQ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TQ6 FirstGlance]. <br> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Arcfu]] | [[Category: Arcfu]] | ||
[[Category: Large Structures]] | |||
[[Category: Bai, Y]] | [[Category: Bai, Y]] | ||
[[Category: Huang, H]] | [[Category: Huang, H]] | ||
Revision as of 13:17, 25 December 2019
Structure of a UbiA homolog from Archaeoglobus fulgidus bound to Cd2+Structure of a UbiA homolog from Archaeoglobus fulgidus bound to Cd2+
Structural highlights
Publication 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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