This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1lgy

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:09, 3 April 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1lgy.jpg|left|200px]]
 
-
{{Structure
+
==LIPASE II FROM RHIZOPUS NIVEUS==
-
|PDB= 1lgy |SIZE=350|CAPTION= <scene name='initialview01'>1lgy</scene>, resolution 2.2&Aring;
+
<StructureSection load='1lgy' size='340' side='right'caption='[[1lgy]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
-
|SITE= <scene name='pdbsite=CAT:Catalytic+Site'>CAT</scene>
+
== Structural highlights ==
-
|LIGAND=
+
<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>
-
|ACTIVITY= [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]
+
</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>
-
|GENE=
+
<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/initialview01.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].
 +
<div style="clear:both"></div>
-
'''LIPASE II FROM RHIZOPUS NIVEUS'''
+
==See Also==
-
 
+
*[[Lipase 3D Structures|Lipase 3D Structures]]
-
 
+
__TOC__
-
==Overview==
+
</StructureSection>
-
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.
+
[[Category: Large Structures]]
-
 
+
-
==About this Structure==
+
-
1LGY is a [[Single protein]] structure of sequence from [http://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].
+
-
 
+
-
==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:[http://www.ncbi.nlm.nih.gov/pubmed/8902613 8902613]
+
[[Category: Rhizopus niveus]]
[[Category: Rhizopus niveus]]
-
[[Category: Single protein]]
+
[[Category: Funatsu J]]
-
[[Category: Triacylglycerol lipase]]
+
[[Category: Kohno M]]
-
[[Category: Funatsu, J.]]
+
[[Category: Kugimiya W]]
-
[[Category: Kohno, M.]]
+
[[Category: Matsuo T]]
-
[[Category: Kugimiya, W.]]
+
[[Category: Mikami B]]
-
[[Category: Matsuo, T.]]
+
[[Category: Morita Y]]
-
[[Category: Mikami, B.]]
+
-
[[Category: Morita, Y.]]
+
-
[[Category: hydrolase (carboxylic ester)]]
+
-
[[Category: lipase]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:30:46 2008''
+

Current revision

LIPASE II FROM RHIZOPUS NIVEUS

PDB ID 1lgy

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1lgy"
Personal tools