7E3V

Metallo beta-lactamase fold protein (cAMP free)

「6L7F」から置き換えられました

7E3V の概要

• エントリーDOI: 10.2210/pdb7e3v/pdb
• 分子名称: UPF0173 metal-dependent hydrolase C7P97_11315, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: dnase, rnase, phosphodiesterase, metal binding protein
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 165104.84

構造登録者

Lee, K.-Y.,Kim, D.-G.,Lee, B.-J. (登録日: 2021-02-09, 公開日: 2022-02-23, 最終更新日: 2023-11-29)

主引用文献

Kim, D.G.,Lee, K.Y.,Lee, S.J.,Cheon, S.H.,Choi, Y.,Lee, H.H.,Ahn, H.C.,Lee, B.J.
Structural and functional studies of SAV1707 from Staphylococcus aureus elucidate its distinct metal-dependent activity and a crucial residue for catalysis.
Acta Crystallogr D Struct Biol, 77:587-598, 2021

PubMed Abstract: The metallo-β-lactamase fold is the most abundant metal-binding domain found in two major kingdoms: bacteria and archaea. Despite the rapid growth in genomic information, most of these enzymes, which may play critical roles in cellular metabolism, remain uncharacterized in terms of structure and function. In this study, X-ray crystal structures of SAV1707, a hypothetical metalloenzyme from Staphylococcus aureus, and its complex with cAMP are reported at high resolutions of 2.05 and 1.55 Å, respectively, with a detailed atomic description. Through a functional study, it was verified that SAV1707 has Ni-dependent phosphodiesterase activity and Mn-dependent endonuclease activity, revealing a different metal selectivity depending on the reaction. In addition, the crystal structure of cAMP-bound SAV1707 shows a unique snapshot of cAMP that reveals the binding mode of the intermediate, and a key residue Phe511 that forms π-π interactions with cAMP was verified as contributing to substrate recognition by functional studies of its mutant. Overall, these findings characterized the relationship between the structure and function of SAV1707 and may provide further understanding of metalloenzymes possessing the metallo-β-lactamase fold.

PubMed: 33950015
DOI: 10.1107/S2059798321001923

実験手法

X-RAY DIFFRACTION (2.05 Å)