3aqu

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Crystal structure of a class V chitinase from Arabidopsis thaliana

Structural highlights

3aqu is a 4 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.01Å
Ligands:FLC
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CHIC_ARATH Can hydrolyze glycol chitin and chitin oligosaccharides (e.g. N-acetylglucosamine) (GlcNAc)4, (GlcNAc)5 and (GlcNAc)6 (PubMed:21390509, PubMed:22936594). Hydrolyzes N-acetylglucosamine oligomers producing dimers from the non-reducing end of the substrates (PubMed:21390509).[1] [2]

Publication Abstract from PubMed

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 A resolution. AtChiC was found to adopt an (beta/alpha)(8) fold with a small insertion domain composed of an alpha-helix and a five-stranded beta-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.

A class V chitinase from Arabidopsis thaliana: gene responses, enzymatic properties, and crystallographic analysis.,Ohnuma T, Numata T, Osawa T, Mizuhara M, Lampela O, Juffer AH, Skriver K, Fukamizo T Planta. 2011 Jul;234(1):123-37. Epub 2011 Mar 9. PMID:21390509[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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References

  1. Ohnuma T, Numata T, Osawa T, Mizuhara M, Lampela O, Juffer AH, Skriver K, Fukamizo T. A class V chitinase from Arabidopsis thaliana: gene responses, enzymatic properties, and crystallographic analysis. Planta. 2011 Jul;234(1):123-37. Epub 2011 Mar 9. PMID:21390509 doi:10.1007/s00425-011-1390-3
  2. Umemoto N, Ohnuma T, Mizuhara M, Sato H, Skriver K, Fukamizo T. Introduction of a tryptophan side chain into subsite +1 enhances transglycosylation activity of a GH-18 chitinase from Arabidopsis thaliana, AtChiC. Glycobiology. 2013 Jan;23(1):81-90. PMID:22936594 doi:10.1093/glycob/cws125
  3. Ohnuma T, Numata T, Osawa T, Mizuhara M, Lampela O, Juffer AH, Skriver K, Fukamizo T. A class V chitinase from Arabidopsis thaliana: gene responses, enzymatic properties, and crystallographic analysis. Planta. 2011 Jul;234(1):123-37. Epub 2011 Mar 9. PMID:21390509 doi:10.1007/s00425-011-1390-3

Contents


PDB ID 3aqu

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