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3AQU

Crystal structure of a class V chitinase from Arabidopsis thaliana

Summary for 3AQU
Entry DOI10.2210/pdb3aqu/pdb
DescriptorAt4g19810, CITRATE ANION (3 entities in total)
Functional Keywordsstress response, tim barrel, hydrolase, chitin
Biological sourceArabidopsis thaliana (thale-cress)
Total number of polymer chains4
Total formula weight155262.60
Authors
Numata, T.,Ohnuma, T.,Osawa, T.,Fukamizo, T. (deposition date: 2010-11-19, release date: 2011-07-20, Last modification date: 2023-11-01)
Primary citationOhnuma, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.01 Å)
Structure validation

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