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PMID: 8070556 Published · ppublish English Comparative Study Journal Article Review

Structural features of plant chitinases and chitin-binding proteins.

FEBS letters ·Vol. 350 ·No. 2-3 ·1994-08-22 ·Pages 159-63

Beintema JJ

Abstract

Structural features of plant chitinases and chitin-binding proteins are discussed. Many of these proteins consist of multiple domains, of which the chitin-binding hevein domain is a predominant one. X-ray and NMR structures of representatives of the major classes of these proteins are available now, and are used to describe the structures of the other ones. Conserved positions of Cys residues can be taken as evidence for identically located disulfide bridges or cysteine residues. The current classification of chitinases is unsatisfactory and needs to be replaced by an evolutionarily more correct one. As the currently known three-dimensional structures of chitinases are those from barley and the rubber tree, Hevea brasiliensis, it is proposed to adopt the designation b-type (classes I, II and IV) and h-type (classes III and V) chitinases, respectively.

MeSH Terms
Amino Acid Sequence Antimicrobial Cationic Peptides Chitin/chemistry Chitinases/chemistry Lectins/chemistry Molecular Sequence Data Plant Lectins Plant Proteins/chemistry Protein Binding Sequence Alignment Sequence Homology, Amino Acid Wheat Germ Agglutinins/chemistry
Chemicals
Antimicrobial Cationic Peptides Lectins Plant Lectins Plant Proteins Wheat Germ Agglutinins hevein Chitin Chitinases
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Beintema J J
Department of Biochemistry, Rijksuniversiteit Groningen, The Netherlands.
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1994-08-22
Pages
159-63
Language
English
Region
England
NLM ID
0155157
Subset
IM
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