1YUM

Crystal Structure of Nicotinic Acid Mononucleotide Adenylyltransferase from Pseudomonas aeruginosa

1YUM の概要

• エントリーDOI: 10.2210/pdb1yum/pdb
• 関連するPDBエントリー: 1YUL 1YUN
• 分子名称: 'Probable nicotinate-nucleotide adenylyltransferase, CITRIC ACID, NICOTINATE MONONUCLEOTIDE, ... (4 entities in total)
• 機能のキーワード: alpha/beta domain, transferase
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 110408.44

構造登録者

Yoon, H.J.,Kim, H.L.,Mikami, B.,Suh, S.W. (登録日: 2005-02-14, 公開日: 2005-11-08, 最終更新日: 2024-04-03)

主引用文献

Yoon, H.J.,Kim, H.L.,Mikami, B.,Suh, S.W.
Crystal structure of nicotinic acid mononucleotide adenylyltransferase from Pseudomonas aeruginosa in its Apo and substrate-complexed forms reveals a fully open conformation
J.Mol.Biol., 351:258-265, 2005

PubMed Abstract: The enzyme nicotinic acid mononucleotide adenylyltransferase (NaMN AT; EC 2.7.7.18) is essential for the synthesis of nicotinamide adenine dinucleotide and is a potential target for antibiotics. It catalyzes the transfer of an AMP moiety from ATP to nicotinic acid mononucleotide to form nicotinic acid adenine dinucleotide. In order to provide missing structural information on the substrate complexes of NaMN AT and to assist structure-based design of specific inhibitors for antibacterial discovery, we have determined the crystal structure of NaMN AT from Pseudomonas aeruginosa in three distinct states, i.e. the NaMN-bound form at 1.7A resolution and ATP-bound form at 2.0A as well as its apo-form at 2.0A. They represent crucial structural information necessary for better understanding of the substrate recognition and the catalytic mechanism. The substrate-unbound and substrate-complexed structures are all in the fully open conformation and there is little conformational change upon binding each of the substrates. Our structures indicate that a conformational change is necessary to bring the two substrates closer together for initiating the catalysis. We suggest that such a conformational change likely occurs only after both substrates are simultaneously bound in the active site.

PubMed: 16009375
DOI: 10.1016/j.jmb.2005.06.001

実験手法

X-RAY DIFFRACTION (1.7 Å)