4TQ4

Structure of a UbiA homolog from Archaeoglobus fulgidus bound to DMAPP and Mg2+

4TQ4 の概要

• エントリーDOI: 10.2210/pdb4tq4/pdb
• 関連するPDBエントリー: 4TQ3 4TQ5 4TQ6
• 分子名称: prenyltransferase, MAGNESIUM ION, DIMETHYLALLYL DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: prenyltransferase, transferase, membrane protein, structural genomics, new york consortium on membrane protein structure, nycomps, psi-biology
• 由来する生物種: Archaeoglobus fulgidus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 134751.54

構造登録者

Huang, H.,Levin, E.J.,Bai, Y.,Zhou, M.,New York Consortium on Membrane Protein Structure (NYCOMPS) (登録日: 2014-06-10, 公開日: 2014-07-16, 最終更新日: 2023-09-27)

主引用文献

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

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: 25051182
DOI: 10.1371/journal.pbio.1001911

実験手法

X-RAY DIFFRACTION (2.5025 Å)