8QJO

SmNuc1 nuclease from Stenotrophomonas maltophilia in complex with guanosine-5'-monophosphate

8QJO の概要

• エントリーDOI: 10.2210/pdb8qjo/pdb
• 分子名称: S1/P1 Nuclease, CHLORIDE ION, ZINC ION, ... (11 entities in total)
• 機能のキーワード: nuclease, hydrolase
• 由来する生物種: Stenotrophomonas maltophilia
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 60448.71

構造登録者

Adamkova, K.,Koval, T.,Kolenko, P.,Dohnalek, J. (登録日: 2023-09-13, 公開日: 2024-09-25, 最終更新日: 2025-01-15)

主引用文献

Adamkova, K.,Trundova, M.,Koval, T.,Hustakova, B.,Kolenko, P.,Duskova, J.,Skalova, T.,Dohnalek, J.
Substrate preference, RNA binding and active site versatility of Stenotrophomonas maltophilia nuclease SmNuc1, explained by a structural study.
Febs J., 292:129-152, 2025

PubMed Abstract: Nucleases of the S1/P1 family have important applications in biotechnology and molecular biology. We have performed structural analyses of SmNuc1 nuclease from Stenotrophomonas maltophilia, including RNA cleavage product binding and mutagenesis in a newly discovered flexible Arg74-motif, involved in substrate binding and product release and likely contributing to the high catalytic rate. The Arg74Gln mutation shifts substrate preference towards RNA. Purine nucleotide binding differs compared to pyrimidines, confirming the plasticity of the active site. The enzyme-product interactions indicate a gradual, stepwise product release. The activity of SmNuc1 towards c-di-GMP in crystal resulted in a distinguished complex with the emerging product 5'-GMP. This enzyme from an opportunistic pathogen relies on specific architecture enabling high performance under broad conditions, attractive for biotechnologies.

PubMed: 39361520
DOI: 10.1111/febs.17265

実験手法

X-RAY DIFFRACTION (1.85 Å)