Journal
JOURNAL OF STRUCTURAL BIOLOGY
Volume 166, Issue 1, Pages 79-87Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jsb.2008.12.010
Keywords
Antheraea mylitta; Canonical protease inhibitor; Reactive site; Disulfide linkage; Fungal protease inhibitor
Funding
- Indian Council of Medical Research, Government of India
- Department of Biotechnology, India
- Council of Scientific and Industrial Research (India)
- International Senior Research Fellow (ISRF) of the Welcome Trust, UK
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Indian tasar silk is produced by a wild insect called Antheraea mylitta. Insects do not have any antigen-antibody mediated immune system like vertebrates but they produce a wide variety of effector proteins and peptides possessing potent antifungal and antibacterial activity to combat microbial attack. Antheraea mylitta expresses a fungal protease inhibitor AmFPI-1, in the hemolymph that inhibits alkaline protease of Aspergillus oryzae for protection against fungal infection. AmFPI-1 is purified from the hemolymph, crystallized and the structure is solved using the single isomorphous replacement with anomalous scattering (SIRAS) method to a resolution of 2.1 angstrom. AmFPI-1 is a single domain protein possessing a unique fold that consists of three helices and five p strands stabilized by a network of six disulfide bonds. The reactive site of AmFPI-1 is located in the loop formed by residues 46-66, wherein Lys54 is the P-1 residue. Superimposition of the loop with reactive sites of other canonical protease inhibitors shows that reactive site conformation of AmFPI-1 is similar to them. The structure of AmFPI-1 provides a framework for the docking of a 1:1 complex between AmFPI-1 and alkaline protease. This study addresses the structural basis of AmFPI-1's specificity towards a fungal serine protease but not to mammalian trypsin and may help in designing specific inhibitors against fungal proteases. (C) 2009 Elsevier Inc. All rights reserved.
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