7OS5

Crystal structure of Rhizobium etli inducible L-asparaginase ReAV (orthorhombic form OP)

これはPDB形式変換不可エントリーです。

7OS5 の概要

• エントリーDOI: 10.2210/pdb7os5/pdb
• 関連するPDBエントリー: 7OS3 7OS6 7OU1
• 分子名称: L-asparaginase, ZINC ION, 1,2-ETHANEDIOL, ... (6 entities in total)
• 機能のキーワード: l-asparaginase, amidohydrolase, rhizobium etli, hydrolase
• 由来する生物種: Rhizobium etli (strain CFN 42 / ATCC 51251)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 80392.77

構造登録者

Loch, J.I.,Imiolczyk, B.,Gilski, M.,Jaskolski, M. (登録日: 2021-06-07, 公開日: 2021-11-24, 最終更新日: 2024-11-06)

主引用文献

Loch, J.I.,Imiolczyk, B.,Sliwiak, J.,Wantuch, A.,Bejger, M.,Gilski, M.,Jaskolski, M.
Crystal structures of the elusive Rhizobium etli L-asparaginase reveal a peculiar active site.
Nat Commun, 12:6717-6717, 2021

PubMed Abstract: Rhizobium etli, a nitrogen-fixing bacterial symbiont of legume plants, encodes an essential L-asparaginase (ReAV) with no sequence homology to known enzymes with this activity. High-resolution crystal structures of ReAV show indeed a structurally distinct, dimeric enzyme, with some resemblance to glutaminases and β-lactamases. However, ReAV has no glutaminase or lactamase activity, and at pH 9 its allosteric asparaginase activity is relatively high, with K for L-Asn at 4.2 mM and k of 438 s. The active site of ReAV, deduced from structural comparisons and confirmed by mutagenesis experiments, contains a highly specific Zn binding site without a catalytic role. The extensive active site includes residues with unusual chemical properties. There are two Ser-Lys tandems, all connected through a network of H-bonds to the Zn center, and three tightly bound water molecules near Ser48, which clearly indicate the catalytic nucleophile.

PubMed: 34795296
DOI: 10.1038/s41467-021-27105-x

実験手法

X-RAY DIFFRACTION (1.293 Å)