1lgy

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{{STRUCTURE_1lgy| PDB=1lgy | SCENE= }}
{{STRUCTURE_1lgy| PDB=1lgy | SCENE= }}
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'''LIPASE II FROM RHIZOPUS NIVEUS'''
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===LIPASE II FROM RHIZOPUS NIVEUS===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 8902613 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8902613}}
==About this Structure==
==About this Structure==
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[[Category: Morita, Y.]]
[[Category: Morita, Y.]]
[[Category: Lipase]]
[[Category: Lipase]]
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Revision as of 17:53, 2 July 2008

Image:1lgy.png

Template:STRUCTURE 1lgy

LIPASE II FROM RHIZOPUS NIVEUS

Template:ABSTRACT PUBMED 8902613

About this Structure

1LGY is a Single protein structure of sequence from Rhizopus niveus. 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. 1996 Sep;120(3):505-10. PMID:8902613

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