Literature DB >> 8119396

Structural similarity of plant chitinase and lysozymes from animals and phage. An evolutionary connection.

L Holm1, C Sander.   

Abstract

A search in the database of known three-dimensional protein structures with the structure of a plant endochitinase revealed a subtle but unambiguous similarity to lysozymes from animals and phages. An evolutionary connection between plant endochitinases and lysozymes is supported by similar overall topology of fold, overlapping substrate specificities and remarkable conservation of some sequence and architectural detail around the active site. Much of the knowledge about lysozyme can now be extended by analogy to endochitinase. New insights into the mechanism of endochitinase are expected to stimulate genetic engineering studies into plant defense mechanisms against pests and pathogens.

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Year:  1994        PMID: 8119396     DOI: 10.1016/0014-5793(94)80187-8

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  16 in total

1.  A family of lysozyme-like virulence factors in bacterial pathogens of plants and animals.

Authors:  A R Mushegian; K J Fullner; E V Koonin; E W Nester
Journal:  Proc Natl Acad Sci U S A       Date:  1996-07-09       Impact factor: 11.205

2.  Fold assessment for comparative protein structure modeling.

Authors:  Francisco Melo; Andrej Sali
Journal:  Protein Sci       Date:  2007-09-28       Impact factor: 6.725

3.  Crystallization and preliminary X-ray diffraction studies of the catalytic domain of a novel chitinase, a member of GH family 23, from the moderately thermophilic bacterium Ralstonia sp. A-471.

Authors:  Nobuo Okazaki; Takao Arimori; Masami Nakazawa; Kazutaka Miyatake; Mitsuhiro Ueda; Taro Tamada
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2011-03-26

4.  Crystal structures of the catalytic domain of a novel glycohydrolase family 23 chitinase from Ralstonia sp. A-471 reveals a unique arrangement of the catalytic residues for inverting chitin hydrolysis.

Authors:  Takao Arimori; Noriko Kawamoto; Shoko Shinya; Nobuo Okazaki; Masami Nakazawa; Kazutaka Miyatake; Tamo Fukamizo; Mitsuhiro Ueda; Taro Tamada
Journal:  J Biol Chem       Date:  2013-05-08       Impact factor: 5.157

5.  The sex-inducing pheromone and wounding trigger the same set of genes in the multicellular green alga Volvox.

Authors:  P Amon; E Haas; M Sumper
Journal:  Plant Cell       Date:  1998-05       Impact factor: 11.277

6.  Heterologous expression and characterization of wild-type and mutant forms of a 26 kDa endochitinase from barley (Hordeum vulgare L.).

Authors:  M D Andersen; A Jensen; J D Robertus; R Leah; K Skriver
Journal:  Biochem J       Date:  1997-03-15       Impact factor: 3.857

7.  Families, superfamilies and subfamilies of glycosyl hydrolases.

Authors:  B Henrissat; A Romeu
Journal:  Biochem J       Date:  1995-10-01       Impact factor: 3.857

8.  Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.

Authors:  B Henrissat; I Callebaut; S Fabrega; P Lehn; J P Mornon; G Davies
Journal:  Proc Natl Acad Sci U S A       Date:  1995-07-18       Impact factor: 11.205

9.  Functional analyses of the chitin-binding domains and the catalytic domain of Brassica juncea chitinase BjCHI1.

Authors:  Ce Mun Tang; Mee-Len Chye; Sathishkumar Ramalingam; Shi-Wen Ouyang; Kai-Jun Zhao; Wimal Ubhayasekera; Sherry L Mowbray
Journal:  Plant Mol Biol       Date:  2004-09       Impact factor: 4.076

10.  Structural relationships in the lysozyme superfamily: significant evidence for glycoside hydrolase signature motifs.

Authors:  Alexandre Wohlkönig; Joëlle Huet; Yvan Looze; René Wintjens
Journal:  PLoS One       Date:  2010-11-09       Impact factor: 3.240

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