View source for 1lgy


==LIPASE II FROM RHIZOPUS NIVEUS==
<StructureSection load='1lgy' size='340' side='right'caption='[[1lgy]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1lgy]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhizopus_niveus Rhizopus niveus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LGY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LGY FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lgy OCA], [https://pdbe.org/1lgy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lgy RCSB], [https://www.ebi.ac.uk/pdbsum/1lgy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lgy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LIP_RHINI LIP_RHINI] Hydrolyzes ester bonds of triglycerides as well as of their derived partial glycerides with a strong 1,3-positional specificity.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lg/1lgy_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lgy ConSurf].
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== Publication Abstract from PubMed ==
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.

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<ref>PMID:8902613</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Lipase 3D Structures|Lipase 3D Structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Rhizopus niveus]]
[[Category: Funatsu J]]
[[Category: Kohno M]]
[[Category: Kugimiya W]]
[[Category: Matsuo T]]
[[Category: Mikami B]]
[[Category: Morita Y]]