6a12: Difference between revisions
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<StructureSection load='6a12' size='340' side='right' caption='[[6a12]], [[Resolution|resolution]] 2.15Å' scene=''> | <StructureSection load='6a12' size='340' side='right' caption='[[6a12]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6a12]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A12 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A12 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6a12]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43513 Atcc 43513]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A12 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A12 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='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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lipA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=33941 ATCC 43513])</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=6a12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a12 OCA], [http://pdbe.org/6a12 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a12 RCSB], [http://www.ebi.ac.uk/pdbsum/6a12 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a12 ProSAT]</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=6a12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a12 OCA], [http://pdbe.org/6a12 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a12 RCSB], [http://www.ebi.ac.uk/pdbsum/6a12 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a12 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Thermo-alkalophilic bacterium, Geobacillus thermoleovorans secrets many enzymes including a 43kDa extracellular lipase. Significant thermostability, organic solvent stability and wide substrate preferences for hydrolysis drew our attention to solve its structure by crystallography. The structure was solved by molecular replacement method and refined up to 2.14A resolution. Structure of the lipase showed an alpha-beta fold with 19 alpha-helices and 10 beta-sheets. The active site remains covered by a lid. One calcium and one zinc atom was found in the crystal. The structure showed a major difference (rmsd 5.6A) from its closest homolog in the amino acid region 191 to 203. Thermal unfolding of the lipase showed that the lipase is highly stable with Tm of 76 degrees C. (13)C NMR spectra of products upon triglyceride hydrolysate revealed that the lipase hydrolyses at both sn-1 and sn-2 positions with equal efficiency. | |||
X-ray structure and characterization of a thermostable lipase from Geobacillus thermoleovorans.,Moharana TR, Pal B, Rao NM Biochem Biophys Res Commun. 2019 Jan 1;508(1):145-151. doi:, 10.1016/j.bbrc.2018.11.105. Epub 2018 Nov 22. PMID:30471860<ref>PMID:30471860</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6a12" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Lipase|Lipase]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Atcc 43513]] | |||
[[Category: Triacylglycerol lipase]] | [[Category: Triacylglycerol lipase]] | ||
[[Category: Moharana, T R]] | [[Category: Moharana, T R]] | ||
Revision as of 15:28, 16 January 2019
X-ray structure of lipase from Geobacillus thermoleovoransX-ray structure of lipase from Geobacillus thermoleovorans
Structural highlights
Publication Abstract from PubMedThermo-alkalophilic bacterium, Geobacillus thermoleovorans secrets many enzymes including a 43kDa extracellular lipase. Significant thermostability, organic solvent stability and wide substrate preferences for hydrolysis drew our attention to solve its structure by crystallography. The structure was solved by molecular replacement method and refined up to 2.14A resolution. Structure of the lipase showed an alpha-beta fold with 19 alpha-helices and 10 beta-sheets. The active site remains covered by a lid. One calcium and one zinc atom was found in the crystal. The structure showed a major difference (rmsd 5.6A) from its closest homolog in the amino acid region 191 to 203. Thermal unfolding of the lipase showed that the lipase is highly stable with Tm of 76 degrees C. (13)C NMR spectra of products upon triglyceride hydrolysate revealed that the lipase hydrolyses at both sn-1 and sn-2 positions with equal efficiency. X-ray structure and characterization of a thermostable lipase from Geobacillus thermoleovorans.,Moharana TR, Pal B, Rao NM Biochem Biophys Res Commun. 2019 Jan 1;508(1):145-151. doi:, 10.1016/j.bbrc.2018.11.105. Epub 2018 Nov 22. PMID:30471860[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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