1GZU

Crystal Structure of Human Nicotinamide Mononucleotide Adenylyltransferase in Complex with NMN

「1GRY」から置き換えられました

1GZU の概要

• エントリーDOI: 10.2210/pdb1gzu/pdb
• 関連するPDBエントリー: 1GRY
• 分子名称: NICOTINAMIDE MONONUCLEOTIDE ADENYLYL TRANSFERASE, BETA-NICOTINAMIDE RIBOSE MONOPHOSPHATE (2 entities in total)
• 機能のキーワード: transferase, nad biosynthesis, adenylyltransferase
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 101338.90

構造登録者

Werner, E.,Ziegler, M.,Lerner, F.,Schweiger, M.,Heinemann, U. (登録日: 2002-06-06, 公開日: 2002-07-05, 最終更新日: 2024-11-13)

主引用文献

Werner, E.,Ziegler, M.,Lerner, F.,Schweiger, M.,Heinemann, U.
Crystal structure of human nicotinamide mononucleotide adenylyltransferase in complex with NMN.
FEBS Lett., 516:239-244, 2002

PubMed Abstract: The final step in the biosynthesis of nicotinamide-adenine dinucleotide, a major coenzyme in cellular redox reactions and involved in intracellular signaling, is catalyzed by the enzyme nicotinamide mononucleotide adenylyltransferase (NMNAT). The X-ray structure of human NMNAT in complex with nicotinamide mononucleotide was solved by the single-wavelength anomalous dispersion method at a resolution of 2.9 A. Human NMNAT is a symmetric hexamer whose subunit is formed by a large six-stranded parallel beta-sheet with helices on both sides. Human NMNAT displays a different oligomerization compared to the archaeal enzyme. The protein-nicotinamide mononucleotide interaction pattern provides insight into ligand binding in the human enzyme.

PubMed: 11959140
DOI: 10.1016/S0014-5793(02)02556-5

実験手法

X-RAY DIFFRACTION (2.9 Å)