Document Detail


Comparison of homology models and crystal structures of cuticle-degrading proteases from nematophagous fungi: structural basis of nematicidal activity.
MedLine Citation:
PMID:  21350115     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Cuticle-degrading proteases secreted by nematophagous fungi can degrade nematode cuticle during infection. Alkaline proteases from nematode-parasitic fungi show stronger nematicidal activity in vitro than neutral proteases from nematode-trapping fungi. Sequence alignment of these proteases revealed that the active-site residues were much conserved. Disulfide bridges in alkaline proteases not only contribute to the thermal stability of enzyme structure but also increase the flexibility of S1 and S4 pockets located at the substrate-binding site. Molecular electrostatic potential surfaces of these proteases change gradually from negative to positive while arranging in the order from neutral to alkaline proteases, possibly contributing to the distinct extent of substrate (nematode cuticle) attraction by proteases. The differences in flexibility of substrate-binding site and in electrostatic surface potential distribution between neutral and alkaline cuticle-degrading proteases are associated with the changes of their catalytic activities and nematicidal activities with fungal species. Our results indicate that nematode-parasitic and nematode-trapping fungi have evolved for distinct adaptation under selective pressure.
Authors:
Lianming Liang; Shuqun Liu; Jinkui Yang; Zhaohui Meng; Liping Lei; Keqin Zhang
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2011-02-24
Journal Detail:
Title:  FASEB journal : official publication of the Federation of American Societies for Experimental Biology     Volume:  25     ISSN:  1530-6860     ISO Abbreviation:  FASEB J.     Publication Date:  2011 Jun 
Date Detail:
Created Date:  2011-05-30     Completed Date:  2011-08-18     Revised Date:  2012-02-15    
Medline Journal Info:
Nlm Unique ID:  8804484     Medline TA:  FASEB J     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1894-902     Citation Subset:  IM    
Affiliation:
Laboratory for Conservation and Utilization of Bioresources, Yunnan University, Kunming 650091, China.
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MeSH Terms
Descriptor/Qualifier:
Animals
Ascomycota / enzymology*,  genetics,  pathogenicity
Gene Expression Regulation, Fungal / physiology
Integumentary System / physiology
Models, Molecular
Nematoda / microbiology*
Peptide Hydrolases / chemistry,  genetics,  metabolism*
Phylogeny
Protein Conformation
Sequence Alignment
Static Electricity
Surface Properties
Chemical
Reg. No./Substance:
EC 3.4.-/Peptide Hydrolases

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


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