3FWK

Crystal Structure of Candida glabrata FMN Adenylyltransferase

3FWK の概要

• エントリーDOI: 10.2210/pdb3fwk/pdb
• 分子名称: FMN Adenylyltransferase, CHLORIDE ION, beta-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: transferase, fad biosynthesis, alpha/beta protein, rossmann-like fold, apo-form, extended loop region
• 由来する生物種: Candida glabrata (Yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36201.33

構造登録者

Huerta, C.,Borek, D.,Zhang, H. (登録日: 2009-01-18, 公開日: 2009-05-26, 最終更新日: 2024-02-21)

主引用文献

Huerta, C.,Borek, D.,Machius, M.,Grishin, N.V.,Zhang, H.
Structure and mechanism of a eukaryotic FMN adenylyltransferase.
J.Mol.Biol., 389:388-400, 2009

PubMed Abstract: Flavin mononucleotide adenylyltransferase (FMNAT) catalyzes the formation of the essential flavocoenzyme flavin adenine dinucleotide (FAD) and plays an important role in flavocoenzyme homeostasis regulation. By sequence comparison, bacterial and eukaryotic FMNAT enzymes belong to two different protein superfamilies and apparently utilize different sets of active-site residues to accomplish the same chemistry. Here we report the first structural characterization of a eukaryotic FMNAT from the pathogenic yeast Candida glabrata. Four crystal structures of C. glabrata FMNAT in different complexed forms were determined at 1.20-1.95 A resolutions, capturing the enzyme active-site states prior to and after catalysis. These structures reveal a novel flavin-binding mode and a unique enzyme-bound FAD conformation. Comparison of the bacterial and eukaryotic FMNATs provides a structural basis for understanding the convergent evolution of the same FMNAT activity from different protein ancestors. Structure-based investigation of the kinetic properties of FMNAT should offer insights into the regulatory mechanisms of FAD homeostasis by FMNAT in eukaryotic organisms.

PubMed: 19375431
DOI: 10.1016/j.jmb.2009.04.022

実験手法

X-RAY DIFFRACTION (1.2 Å)