1lgy
From Proteopedia
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==Overview== | ==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 . | + | 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== | ==About this Structure== | ||
| - | 1LGY is a | + | 1LGY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhizopus_niveus Rhizopus niveus]. Active as [http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] Structure known Active Site: CAT. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LGY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: lipase]] | [[Category: lipase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:59:12 2007'' |
Revision as of 11:53, 5 November 2007
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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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