1K4M

Crystal structure of E.coli nicotinic acid mononucleotide adenylyltransferase complexed to deamido-NAD

1K4M の概要

• エントリーDOI: 10.2210/pdb1k4m/pdb
• 関連するPDBエントリー: 1k4k
• 分子名称: NaMN adenylyltransferase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, CITRIC ACID, ... (4 entities in total)
• 機能のキーワード: nucleotidyltransferase, transferase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 76228.26

構造登録者

Zhang, H.,Zhou, T.,Kurnasov, O.,Cheek, S.,Grishin, N.V.,Osterman, A. (登録日: 2001-10-08, 公開日: 2002-10-08, 最終更新日: 2023-08-16)

主引用文献

Zhang, H.,Zhou, T.,Kurnasov, O.,Cheek, S.,Grishin, N.V.,Osterman, A.
Crystal structures of E. coli nicotinate mononucleotide adenylyltransferase and its complex with deamido-NAD.
Structure, 10:69-79, 2002

PubMed Abstract: Nicotinamide/Nicotinate mononucleotide (NMN/NaMN) adenylyltransferase is an indispensable enzyme in both de novo biosynthesis and salvage of NAD+ and NADP+. In prokaryotes, it is absolutely required for cell survival, thus representing an attractive target for the development of new broad-spectrum antibacteria inhibitors. The crystal structures of E. coli NaMN adenylyltransferase (NMNAT) and its complex with deamido-NAD (NaAD) revealed that ligand binding causes large conformational changes in several loop regions around the active site. The enzyme specifically recognizes the deamidated pyridine nucleotide through interactions between nicotinate carboxylate with several protein main chain amides and a positive helix dipole. Comparison of E. coli NMNAT with those from archaeal organisms revealed extensive differences in the active site architecture, enzyme-ligand interaction mode, and bound dinucleotide conformations. The bacterial NaMN adenylyltransferase structures described here provide a foundation for structure-based design of specific inhibitors that may have therapeutic potential.

PubMed: 11796112
DOI: 10.1016/S0969-2126(01)00693-1

実験手法

X-RAY DIFFRACTION (1.9 Å)