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4kea

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==Crystal structure of D196N mutant of Monoglyceride lipase from Bacillus sp. H257 in space group P212121==
==Crystal structure of D196N mutant of Monoglyceride lipase from Bacillus sp. H257 in space group P212121==
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<StructureSection load='4kea' size='340' side='right' caption='[[4kea]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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<StructureSection load='4kea' size='340' side='right'caption='[[4kea]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4kea]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Bac25 Bac25]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KEA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KEA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4kea]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._H-257 Bacillus sp. H-257]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KEA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KEA FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ke6|4ke6]], [[4ke7|4ke7]], [[4ke8|4ke8]], [[4ke9|4ke9]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acylglycerol_lipase Acylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.23 3.1.1.23] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4kea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kea OCA], [https://pdbe.org/4kea PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kea RCSB], [https://www.ebi.ac.uk/pdbsum/4kea PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kea ProSAT]</span></td></tr>
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<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=4kea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kea OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kea RCSB], [http://www.ebi.ac.uk/pdbsum/4kea PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/MGLP_BAC25 MGLP_BAC25] Hydrolyzes monoacylglycerols, with the highest activity occurring with 1-monolauroylglycerol.
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Monoacylglycerol lipases (MGLs) play an important role in lipid catabolism across all kingdoms of life by catalyzing the release of free fatty acids from monoacylglycerols. The three-dimensional structures of human and a bacterial MGL were determined only recently as the first members of this lipase family. In addition to the alpha/beta hydrolase core, they showed unexpected structural similarities even in the cap region. Nevertheless, the structural basis for substrate binding and conformational changes of MGLs is poorly understood. Here we present a comprehensive study of five crystal structures of MGL from Bacillus sp. H257 in its free form and in complex with different substrate analogues and the natural substrate 1-lauroyl glycerol (1-LG). The occurrence of different conformations reveals a high degree of conformational plasticity of the cap region. We identify a specific residue, Ile145 that might act as a gate keeper restricting access to the binding site. Site directed mutagenesis of Ile145 leads to significantly reduced hydrolase activity. Bacterial MGL in complex with 1-LG, myristoyl-, palmitoyl and stearoyl-substrate analogues enable identification of the binding sites for the alkyl chain and the glycerol moiety of the natural ligand. They also provide snapshots of the hydrolytic reaction of bMGL at different stages. The alkyl chains are buried in a hydrophobic tunnel in an extended conformation. Binding of the glycerol moiety is mediated via Glu156 and water molecules. Analysis of the structural features responsible for cap plasticity and the binding modes of the ligands suggest conservation of these features also in human MGL.
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Conformational plasticity and ligand binding of bacterial monoacylglycerol lipase.,Rengachari S, Aschauer P, Schittmayer M, Mayer N, Gruber K, Breinbauer R, Birner-Gruenberger R, Dreveny I, Oberer M J Biol Chem. 2013 Sep 6. PMID:24014019<ref>PMID:24014019</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==See Also==
==See Also==
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*[[Lipase|Lipase]]
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*[[Lipase 3D Structures|Lipase 3D Structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Acylglycerol lipase]]
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[[Category: Bacillus sp. H-257]]
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[[Category: Bac25]]
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[[Category: Large Structures]]
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[[Category: Aschauer, P]]
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[[Category: Aschauer P]]
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[[Category: Dreveny, I]]
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[[Category: Dreveny I]]
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[[Category: Gruber, K]]
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[[Category: Gruber K]]
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[[Category: Oberer, M]]
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[[Category: Oberer M]]
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[[Category: Rengachari, S]]
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[[Category: Rengachari S]]
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[[Category: Alpha/beta hydrolase]]
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[[Category: Hydrolase]]
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[[Category: Monoglyceride lipase]]
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Current revision

Crystal structure of D196N mutant of Monoglyceride lipase from Bacillus sp. H257 in space group P212121

PDB ID 4kea

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