1LGY

LIPASE II FROM RHIZOPUS NIVEUS

Summary for 1LGY

• Entry DOI: 10.2210/pdb1lgy/pdb
• Descriptor: TRIACYLGLYCEROL LIPASE (2 entities in total)
• Functional Keywords: lipase, hydrolase (carboxylic ester)
• Biological source: Rhizopus niveus
• Cellular location: Secreted, extracellular space: P61871
• Total number of polymer chains: 3
• Total formula weight: 88870.51

Authors

Kohno, M.,Funatsu, J.,Mikami, B.,Kugimiya, W.,Matsuo, T.,Morita, Y. (deposition date: 1996-05-23, release date: 1996-12-23, Last modification date: 2024-10-30)

Primary citation

Kohno, M.,Funatsu, J.,Mikami, B.,Kugimiya, W.,Matsuo, T.,Morita, Y.
The crystal structure of lipase II from Rhizopus niveus at 2.2 A resolution.
J.Biochem.(Tokyo), 120:505-510, 1996

PubMed Abstract: The crystal and molecular structure of Lipase II from Rhizopus niveus was analyzed using X-ray single crystal diffraction data at a resolution of 2.2 A. The structure was refined to an R-factor of 0.19 for all available data. This lipase was purified and crystallized as Lipase I, which contains two polypeptide chains combined through non-covalent interaction. However, during crystal growth, Lipase I was converted to Lipase II, which consists of a single polypeptide chain of 269 amino acid residues, by limited proteolysis. The structure of Lipase II shows a typical alpha/beta hydrolase fold containing the so-called nucleophilic elbow. The catalytic center of this enzyme is analogous to those of other neutral lipases and serine proteases. This catalytic center is sheltered by an alpha-helix lid, which appears in neutral lipases, opening the active site at the oil-water interface.

PubMed: 8902613

Experimental method

X-RAY DIFFRACTION (2.2 Å)