机构：[1]Laboratory for Conservation and Utilization of Bioresources and Key Laboratory for Microbial Resources of the Ministry of Education, Yunnan University, Kunming, China[2]Laboratory of Molecular Cardiology, Department of Cardiology, First Affiliated Hospital of Kunming Medical University, Kunming, China内科科室心脏内科昆明医科大学附属第一医院[3]Tobacco Agricultural Science Institute of Yunnan Province, Yuxi, China内科科室外科科室干疗科3号楼重症监护病房（ICU）重症医学科昆明医科大学附属第一医院
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.-Liang, L., Liu, S., Yang, J., Meng, Z., Lei, L., Zhang, K. Comparison of homology models and crystal structures of cuticle-degrading proteases from nematophagous fungi: structural basis of nematicidal activity. FASEB J. 25, 1894-1902 (2011). www.fasebj.org
基金：
This work was
jointly funded by the National Basic Research Program of
China (approval 2007CB411600); projects from the National
Natural Science Foundation of China (approvals 30630003,
30860011, 30960229, and 30660107); the Department of
Science and Technology of Yunnan Province (approvals
2007PY-22, 2007C007Z, and 2009CI052); the Yunnan Branch
of China Tobacco Industrial Corporation (grant 2010YN17);
and Yunnan University (grant 2010C02Z).
第一作者机构：[1]Laboratory for Conservation and Utilization of Bioresources and Key Laboratory for Microbial Resources of the Ministry of Education, Yunnan University, Kunming, China
共同第一作者：
通讯作者：
通讯机构：[*1]Laboratory for Conservation and Utilization of Bioresources and Key Laboratory for Microbial Resources of the Ministry of Education, Yunnan University, Kunming 650091, China.
推荐引用方式(GB/T 7714)：
Lianming Liang,Shuqun Liu,Jinkui Yang,et al.Comparison of homology models and crystal structures of cuticle-degrading proteases from nematophagous fungi: structural basis of nematicidal activity[J].FASEB JOURNAL.2011,25(6):1894-1902.doi:10.1096/fj.10-175653.
APA：
Lianming Liang,Shuqun Liu,Jinkui Yang,Zhaohui Meng,Liping Lei&Keqin Zhang.(2011).Comparison of homology models and crystal structures of cuticle-degrading proteases from nematophagous fungi: structural basis of nematicidal activity.FASEB JOURNAL,25,(6)
MLA：
Lianming Liang,et al."Comparison of homology models and crystal structures of cuticle-degrading proteases from nematophagous fungi: structural basis of nematicidal activity".FASEB JOURNAL 25..6(2011):1894-1902
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