4BR7

Legionella pneumophila NTPDase1 crystal form I, open, AMPNP complex

4BR7 の概要

• エントリーDOI: 10.2210/pdb4br7/pdb
• 関連するPDBエントリー: 4BQZ 4BR0 4BR2 4BR4 4BR5 4BR9 4BRA 4BRC 4BRD 4BRE 4BRF 4BRG 4BRH 4BRI 4BRK 4BRL 4BRM 4BRN 4BRO 4BRP 4BRQ
• 分子名称: ECTONUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE I, MAGNESIUM ION, 5'-O-[(R)-hydroxy(phosphonoamino)phosphoryl]adenosine, ... (5 entities in total)
• 機能のキーワード: hydrolase, apyrase, atpase, adpase, cd39, purinergic signalling, domain rotation, transition state, ntpdase
• 由来する生物種: LEGIONELLA PNEUMOPHILA
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 42058.66

構造登録者

Zebisch, M.,Schaefer, P.,Lauble, P.,Straeter, N. (登録日: 2013-06-04, 公開日: 2013-07-17, 最終更新日: 2024-10-23)

主引用文献

Zebisch, M.,Krauss, M.,Schaefer, P.,Lauble, P.,Straeter, N.
Crystallographic Snapshots Along the Reaction Pathway of Nucleoside Triphosphate Diphosphohydrolases
Structure, 21:1460-, 2013

PubMed Abstract: In vertebrates, membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (NTPDases) on the cell surface are responsible for signal conversion and termination in purinergic signaling by extracellular nucleotides. Here we present apo and complex structures of the rat NTPDase2 extracellular domain and Legionella pneumophila NTPDase1, including a high-resolution structure with a transition-state analog. Comparison of ATP and ADP binding modes shows how NTPDases engage the same catalytic site for hydrolysis of nucleoside triphosphates and diphosphates. We find that this dual specificity is achieved at the expense of base specificity. Structural and mutational studies indicate that a conserved active-site water is replaced by the phosphate product immediately after phosphoryl transfer. Partial base specificity for purines in LpNTPDase1 is based on a different intersubunit base binding site for pyrimidine bases. A comparison of the bacterial enzyme in six independent crystal forms shows that NTPDases can undergo a domain closure motion of at least 17°.

PubMed: 23830739
DOI: 10.1016/J.STR.2013.05.016

実験手法

X-RAY DIFFRACTION (1.8 Å)