4fdm: Difference between revisions
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==Crystallization and 3D structure elucidation of thermostable L2 lipase from thermophilic locally isolated Bacillus sp. L2.== | ==Crystallization and 3D structure elucidation of thermostable L2 lipase from thermophilic locally isolated Bacillus sp. L2.== | ||
<StructureSection load='4fdm' size='340' side='right' caption='[[4fdm]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='4fdm' size='340' side='right' caption='[[4fdm]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fdm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fdm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fdm RCSB], [http://www.ebi.ac.uk/pdbsum/4fdm PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fdm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fdm OCA], [http://pdbe.org/4fdm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fdm RCSB], [http://www.ebi.ac.uk/pdbsum/4fdm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fdm ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4fdm" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 18:59, 11 August 2016
Crystallization and 3D structure elucidation of thermostable L2 lipase from thermophilic locally isolated Bacillus sp. L2.Crystallization and 3D structure elucidation of thermostable L2 lipase from thermophilic locally isolated Bacillus sp. L2.
Structural highlights
Publication Abstract from PubMedThe crystallization of proteins makes it possible to determine their structure by X-ray crystallography, and is therefore important for the analysis of protein structure-function relationships. L2 lipase was crystallized by using the J-tube counter diffusion method. A crystallization consisting of 20% PEG 6000, 50 mM MES pH 6.5 and 50 mM NaCl was found to be the best condition to produce crystals with good shape and size (0.5 x 0.1 x 0.2 mm). The protein concentration used for the crystallization was 3 mg/mL. L2 lipase crystal has two crystal forms, Shape 1 and Shape 2. Shape 2 L2 lipase crystal was diffracted at 1.5 A and the crystal belongs to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 72.0, b = 81.8, c = 83.4 A, alpha = beta = gamma = 90 degrees . There is one molecule per asymmetric unit and the solvent content of the crystals is 56.9%, with a Matthew's coefficient of 2.85 A Da(-1). The 3D structure of L2 lipase revealed topological organization of alpha/beta-hydrolase fold consisting of 11 beta-strands and 13 alpha-helices. Ser-113, His-358 and Asp-317 were assigned as catalytic triad residues. One Ca(2+) and one Zn(2+) were found in the L2 lipase molecule. 3D Structure Elucidation of Thermostable L2 Lipase from Thermophilic Bacillus sp. L2.,Abd Rahman RN, Shariff FM, Basri M, Salleh AB Int J Mol Sci. 2012;13(7):9207-17. doi: 10.3390/ijms13079207. Epub 2012 Jul 23. PMID:22942761[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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