3UUF

Crystal structure of mono- and diacylglycerol lipase from Malassezia globosa

Summary for 3UUF

• Entry DOI: 10.2210/pdb3uuf/pdb
• Related: 3UUE
• Descriptor: LIP1, secretory lipase (Family 3), 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose, ... (4 entities in total)
• Functional Keywords: lid-domain, hydrolase
• Biological source: Malassezia globosa (Dandruff-associated fungus)
• Total number of polymer chains: 1
• Total formula weight: 31636.42

Authors

Xu, T.,Xu, J.,Hou, S.,Liu, J. (deposition date: 2011-11-28, release date: 2012-04-25, Last modification date: 2024-11-20)

Primary citation

Xu, T.,Liu, L.,Hou, S.,Xu, J.,Yang, B.,Wang, Y.,Liu, J.
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., 178:363-369, 2012

PubMed 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 Å 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.

PubMed: 22484238
DOI: 10.1016/j.jsb.2012.03.006

Experimental method

X-RAY DIFFRACTION (2.6 Å)