6F4D

Structure of the Y21F variant of quinolinate synthase in complex with PGH

6F4D の概要

• エントリーDOI: 10.2210/pdb6f4d/pdb
• 分子名称: Quinolinate synthase A, IRON/SULFUR CLUSTER, PHOSPHOGLYCOLOHYDROXAMIC ACID, ... (6 entities in total)
• 機能のキーワード: nad biosynthesis, iron sulfur cluster, transferase
• 由来する生物種: Thermotoga maritima
• 細胞内の位置: Cytoplasm : Q9X1X7
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35388.68

構造登録者

Volbeda, A.,Fontecilla-Camps, J.C. (登録日: 2017-11-29, 公開日: 2018-04-25, 最終更新日: 2024-01-17)

主引用文献

Volbeda, A.,Saez Cabodevilla, J.,Darnault, C.,Gigarel, O.,Han, T.H.,Renoux, O.,Hamelin, O.,Ollagnier-de-Choudens, S.,Amara, P.,Fontecilla-Camps, J.C.
Crystallographic Trapping of Reaction Intermediates in Quinolinic Acid Synthesis by NadA.
ACS Chem. Biol., 13:1209-1217, 2018

PubMed Abstract: NadA is a multifunctional enzyme that condenses dihydroxyacetone phosphate (DHAP) with iminoaspartate (IA) to generate quinolinic acid (QA), the universal precursor of the nicotinamide adenine dinucleotide (NAD(P)) cofactor. Using X-ray crystallography, we have (i) characterized two of the reaction intermediates of QA synthesis using a "pH-shift" approach and a slowly reacting Thermotoga maritima NadA variant and (ii) observed the QA product, resulting from the degradation of an intermediate analogue, bound close to the entrance of a long tunnel leading to the solvent medium. We have also used molecular docking to propose a condensation mechanism between DHAP and IA based on two previously published Pyrococcus horikoshi NadA structures. The combination of reported data and our new results provide a structure-based complete catalytic sequence of QA synthesis by NadA.

PubMed: 29641168
DOI: 10.1021/acschembio.7b01104

実験手法

X-RAY DIFFRACTION (2 Å)