1lgy

From Proteopedia

Revision as of 14:37, 5 November 2007

LIPASE II FROM RHIZOPUS NIVEUS

Overview

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.

About this Structure

1LGY is a Single protein structure of sequence from Rhizopus niveus. Active as Triacylglycerol lipase, with EC number 3.1.1.3 Structure known Active Site: CAT. Full crystallographic information is available from OCA.

Reference

The crystal structure of lipase II from Rhizopus niveus at 2.2 A resolution., Kohno M, Funatsu J, Mikami B, Kugimiya W, Matsuo T, Morita Y, J Biochem (Tokyo). 1996 Sep;120(3):505-10. PMID:8902613

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