3AQU

Crystal structure of a class V chitinase from Arabidopsis thaliana

3AQU の概要

• エントリーDOI: 10.2210/pdb3aqu/pdb
• 分子名称: At4g19810, CITRATE ANION (3 entities in total)
• 機能のキーワード: stress response, tim barrel, hydrolase, chitin
• 由来する生物種: Arabidopsis thaliana (thale-cress)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 155262.60

構造登録者

Numata, T.,Ohnuma, T.,Osawa, T.,Fukamizo, T. (登録日: 2010-11-19, 公開日: 2011-07-20, 最終更新日: 2023-11-01)

主引用文献

Ohnuma, T.,Numata, T.,Osawa, T.,Mizuhara, M.,Lampela, O.,Juffer, A.H.,Skriver, K.,Fukamizo, T.
A class V chitinase from Arabidopsis thaliana: gene responses, enzymatic properties, and crystallographic analysis
Planta, 234:123-137, 2011

PubMed Abstract: Expression of a class V chitinase gene (At4g19810, AtChiC) in Arabidopsis thaliana was examined by quantitative real-time PCR and by analyzing microarray data available at Genevestigator. The gene expression was induced by the plant stress-related hormones abscisic acid (ABA) and jasmonic acid (JA) and by the stress resulting from the elicitor flagellin, NaCl, and osmosis. The recombinant AtChiC protein was produced in E. coli, purified, and characterized with respect to the structure and function. The recombinant AtChiC hydrolyzed N-acetylglucosamine oligomers producing dimers from the non-reducing end of the substrates. The crystal structure of AtChiC was determined by the molecular replacement method at 2.0 Å resolution. AtChiC was found to adopt an (β/α)(8) fold with a small insertion domain composed of an α-helix and a five-stranded β-sheet. From docking simulation of AtChiC with pentameric substrate, the amino acid residues responsible for substrate binding were found to be well conserved when compared with those of the class V chitinase from Nicotiana tabacum (NtChiV). All of the structural and functional properties of AtChiC are quite similar to those obtained for NtChiV, and seem to be common to class V chitinases from higher plants.

PubMed: 21390509
DOI: 10.1007/s00425-011-1390-3

実験手法

X-RAY DIFFRACTION (2.01 Å)