1JN9

Structure of Putative Asparaginase Encoded by Escherichia coli ybiK Gene

1JN9 の概要

• エントリーDOI: 10.2210/pdb1jn9/pdb
• 関連するPDBエントリー: 1APY 1APZ 1AYY 2GAC 2GAW 9GAA 9GAC 9GAF
• 分子名称: PUTATIVE L-ASPARAGINASE, SODIUM ION, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: ntn hydrolase, asparaginase, autoproteolysis, hydrolase
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 67081.70

構造登録者

Borek, D.,Jaskolski, M. (登録日: 2001-07-23, 公開日: 2003-09-09, 最終更新日: 2024-10-30)

主引用文献

Michalska, K.,Borek, D.,Hernandez-Santoyo, A.,Jaskolski, M.
Crystal packing of plant-type L-asparaginase from Escherichia coli.
Acta Crystallogr.,Sect.D, 64:309-320, 2008

PubMed Abstract: Plant-type L-asparaginases hydrolyze the side-chain amide bond of L-asparagine or its beta-peptides. They belong to the N-terminal nucleophile (Ntn) hydrolases and are synthesized as inactive precursor molecules. Activation occurs via the autoproteolytic release of two subunits, alpha and beta, the latter of which carries the nucleophile at its N-terminus. Crystallographic studies of plant-type asparaginases have focused on an Escherichia coli homologue (EcAIII), which has been crystallized in several crystal forms. Although they all belong to the same P2 1 2 1 2 1 space group with similar unit-cell parameters, they display different crystal-packing arrangements and thus should be classified as separate polymorphs. This variability stems mainly from different positions of the EcAIII molecules within the unit cell, although they also exhibit slight differences in orientation. The intermolecular interactions that trigger different crystal lattice formation are mediated by ions, which represent the most variable component of the crystallization conditions. This behaviour confirms recent observations that small molecules might promote protein crystal lattice formation.

PubMed: 18323626
DOI: 10.1107/S0907444907068072

実験手法

X-RAY DIFFRACTION (2.3 Å)