Xu_2012_J.Struct.Biol_178_363

Reference

Title : Crystal structure of a mono- and diacylglycerol lipase from Malassezia globosa reveals a novel lid conformation and insights into the substrate specificity - Xu_2012_J.Struct.Biol_178_363
Author(s) : Xu T , Liu L , Hou S , Xu J , Yang B , Wang Y , Liu J
Ref : J Struct Biol , 178 :363 , 2012
Abstract : Most lipases contain a lid domain to shield the hydrophobic binding site from the water environment. The lid, mostly in helical form, can undergo a conformational change to expose the active cleft during the interfacial activation. Here we report the crystal structures of Malassezia globosa LIP1 (SMG1) at 1.45 and 2.60 resolution in two crystal forms. The structures present SMG1 in its closed form, with a novel lid in loop conformation. SMG1 is one of the few members in the fungal lipase family that has been found to be strictly specific for mono- and diacylglycerol. To date, the mechanism for this substrate specificity remains largely unknown. To investigate the substrate binding properties, we built a model of SMG1 in open conformation. Based on this model, we found that the two bulky hydrophobic residues adjacent to the catalytic site and the N-terminal hinge region of the lid both may act as steric hindrances for triacylglycerols binding. These unique structural features of SMG1 will provide a better understanding on the substrate specificity of mono- and diacylglycerol lipases and a platform for further functional study of this enzyme.
ESTHER : Xu_2012_J.Struct.Biol_178_363
PubMedSearch : Xu_2012_J.Struct.Biol_178_363
PubMedID: 22484238
Gene_locus related to this paper: malgo-a8puy1

Related information

Gene_locus related to this paper: malgo-a8puy1

Citations formats

Xu T, Liu L, Hou S, Xu J, Yang B, Wang Y, Liu J (2012)
Crystal structure of a mono- and diacylglycerol lipase from Malassezia globosa reveals a novel lid conformation and insights into the substrate specificity
J Struct Biol 178 :363

Xu T, Liu L, Hou S, Xu J, Yang B, Wang Y, Liu J (2012)
J Struct Biol 178 :363