Monthly Archives: December 2019

Chaperone mechanism of DJ-1

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DJ-1 is a deglycase enzyme which exhibits a redox-sensitive chaperone-like activity. The partially oxidized state of DJ-1 is active in inhibiting the aggregation of α-synuclein, a key protein associated with Parkinson’s disease. The underlying molecular mechanism behind α-synuclein aggregation inhibition remains unknown. Here we report that the partially oxidized DJ-1 possesses an adhesive surface which sequesters […]

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SpaB, an atypically adhesive basal pilin from the lactobacillar SpaCBA pilus: crystallization and X-ray diffraction analysis

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Microbial attachment to host surfaces is a critical step in colonization. Hence, interfering with the initial attachment is considered as one of the attractive and efficient approaches in improving health and combating infections. Towards providing the essential foundations for this approach, Dr Krishnan’s structural biology group currently focus on hair-like surface organelles called pili or […]

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Structural insights into the lipid transfer mechanism of a non-specific lipid transfer protein

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The non-specific lipid transfer protein (nsLTP) transfers a variety of lipids between membranes and plays an important role in membrane biogenesis and regulating intra cellular fatty acid pools. However, the mechanism of lipid transfer remained enigmatic. We co-crystallized lipids with nsLTP under a wide range of conditions and determined crystal structures of four intermediate lipid […]

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Comparative study of 7S globulin from Corylus avellana and Solanum lycopersicum revealed importance of salicylic acid and Cu-binding loop in modulating their function.

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We had recently shown that vicilins could exhibit superoxide dismutase activity. In the present study, we have carried out functional and structural analyses of vicilins from two distinct evolutionary sources – tomato (S. lycopersicum; SL80.1) and hazelnut (C. avellana; HZ.1) – towards understanding the basis of their functional diversity. It was identified that SL80.1 retained […]

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