4TQ5
Structure of a UbiA homolog from Archaeoglobus fulgidus
Summary for 4TQ5
Entry DOI | 10.2210/pdb4tq5/pdb |
Related | 4TQ3 4TQ4 4TQ6 |
Descriptor | prenyltransferase, octyl beta-D-glucopyranoside (2 entities in total) |
Functional Keywords | prenyltransferase, transferase, membrane protein, structural genomics, new york consortium on membrane protein structure, nycomps, psi-biology |
Biological source | Archaeoglobus fulgidus |
Total number of polymer chains | 1 |
Total formula weight | 33966.92 |
Authors | Huang, H.,Levin, E.J.,Bai, Y.,Zhou, M.,New York Consortium on Membrane Protein Structure (NYCOMPS) (deposition date: 2014-06-10, release date: 2014-07-16, Last modification date: 2023-12-27) |
Primary citation | Huang, H.,Levin, E.J.,Liu, S.,Bai, Y.,Lockless, S.W.,Zhou, M. Structure of a Membrane-Embedded Prenyltransferase Homologous to UBIAD1. Plos Biol., 12:e1001911-e1001911, 2014 Cited by PubMed Abstract: 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. PubMed: 25051182DOI: 10.1371/journal.pbio.1001911 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.2023 Å) |
Structure validation
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