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<StructureSection load='2ory' size='340' side='right'caption='[[2ory]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='2ory' size='340' side='right'caption='[[2ory]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2ory]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Photobacterium_sp._m37 Photobacterium sp. m37]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ORY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ORY FirstGlance]. <br>
<table><tr><td colspan='2'>[[2ory]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Photobacterium_sp._M37 Photobacterium sp. M37]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ORY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ORY FirstGlance]. <br>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </span></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]] 2.2&#8491;</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=2ory FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ory OCA], [https://pdbe.org/2ory PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ory RCSB], [https://www.ebi.ac.uk/pdbsum/2ory PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ory 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=2ory FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ory OCA], [https://pdbe.org/2ory PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ory RCSB], [https://www.ebi.ac.uk/pdbsum/2ory PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ory ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5DRN8_9GAMM Q5DRN8_9GAMM]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=2ory ConSurf].
</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=2ory ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The M37 lipase from Photobacterium lipolyticum shows an extremely low activation energy and strong activity at low temperatures, with optimum activity seen at 298 K and more than 75% of the optimum activity retained down to 278 K. Though the M37 lipase is most closely related to the filamentous fungal lipase, Rhizomucor miehei lipase (RML) at the primary structure level, their activity characteristics are completely different. In an effort to identify structural components of cold adaptation in lipases, we determined the crystal structure of the M37 lipase at 2.2 A resolution and compared it to that of nonadapted RML. Structural analysis revealed that M37 lipase adopted a folding pattern similar to that observed for other lipase structures. However, comparison with RML revealed that the region beneath the lid of the M37 lipase included a significant and unique cavity that would be occupied by a lid helix upon substrate binding. In addition, the oxyanion hole was much wider in M37 lipase than RML. We propose that these distinct structural characteristics of M37 lipase may facilitate the lateral movement of the helical lid and subsequent substrate hydrolysis, which might explain its low activation energy and high activity at low temperatures. Proteins 2008. (c) 2008 Wiley-Liss, Inc.
Structural basis for the cold adaptation of psychrophilic M37 lipase from Photobacterium lipolyticum.,Jung SK, Jeong DG, Lee MS, Lee JK, Kim HK, Ryu SE, Park BC, Kim JH, Kim SJ Proteins. 2008 Jan 10;71(1):476-484. PMID:18186467<ref>PMID:18186467</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2ory" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Lipase 3D Structures|Lipase 3D Structures]]
*[[Lipase 3D Structures|Lipase 3D Structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Photobacterium sp. m37]]
[[Category: Photobacterium sp. M37]]
[[Category: Triacylglycerol lipase]]
[[Category: Jeong DG]]
[[Category: Jeong, D G]]
[[Category: Jung SK]]
[[Category: Jung, S K]]
[[Category: Kim SJ]]
[[Category: Kim, S J]]
[[Category: Alpha/beta hydrolase]]
[[Category: Hydrolase]]

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