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| <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=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[4fdm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_sp._l2 Bacillus sp. l2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FDM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FDM FirstGlance]. <br> | | <table><tr><td colspan='2'>[[4fdm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._L2 Bacillus sp. L2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FDM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FDM FirstGlance]. <br> |
| </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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4fdm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fdm OCA], [https://pdbe.org/4fdm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fdm RCSB], [https://www.ebi.ac.uk/pdbsum/4fdm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fdm ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/Q5I4I3_9BACI Q5I4I3_9BACI] |
| The 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.
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| 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<ref>PMID:22942761</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 4fdm" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Bacillus sp. l2]] | | [[Category: Bacillus sp. L2]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Triacylglycerol lipase]]
| | [[Category: Basri MB]] |
| [[Category: Basri, M B]] | | [[Category: Rahman RNZRA]] |
| [[Category: Rahman, R N.Z R.A]] | | [[Category: Salleh AB]] |
| [[Category: Salleh, A B]] | | [[Category: Shariff FM]] |
| [[Category: Shariff, F M]] | |
| [[Category: Hydrolase]]
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| [[Category: Thermostable lipase]]
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