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1tia
From Proteopedia
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==AN UNUSUAL BURIED POLAR CLUSTER IN A FAMILY OF FUNGAL LIPASES== | ==AN UNUSUAL BURIED POLAR CLUSTER IN A FAMILY OF FUNGAL LIPASES== | ||
| - | <StructureSection load='1tia' size='340' side='right' caption='[[1tia]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='1tia' size='340' side='right'caption='[[1tia]], [[Resolution|resolution]] 2.10Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1tia]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1tia]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Penicillium_camemberti Penicillium camemberti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TIA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TIA FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tia FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tia OCA], [https://pdbe.org/1tia PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tia RCSB], [https://www.ebi.ac.uk/pdbsum/1tia PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tia ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/MDLA_PENCA MDLA_PENCA] Hydrolyzes mono- and diacylglycerol but not triacylglycerol. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ti/1tia_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ti/1tia_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| - | </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/ | + | </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=1tia ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The stability of globular proteins arises largely from the burial of non-polar amino acids in their interior. These residues are efficiently packed to eliminate energetically unfavorable cavities. Contrary to these observations, high resolution X-ray crystallographic analyses of four homologous lipases from filamentous fungi reveal an alpha/beta fold which contains a buried conserved constellation of charged and polar side chains with associated cavities containing ordered water molecules. It is possible that this structural arrangement plays an important role in interfacial catalysis. | ||
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| - | An unusual buried polar cluster in a family of fungal lipases.,Derewenda U, Swenson L, Green R, Wei Y, Dodson GG, Yamaguchi S, Haas MJ, Derewenda ZS Nat Struct Biol. 1994 Jan;1(1):36-47. PMID:7656005<ref>PMID:7656005</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
==See Also== | ==See Also== | ||
| - | *[[Lipase|Lipase]] | + | *[[Lipase 3D Structures|Lipase 3D Structures]] |
| - | + | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Penicillium camemberti]] | [[Category: Penicillium camemberti]] | ||
| - | + | [[Category: Derewenda U]] | |
| - | [[Category: Derewenda | + | [[Category: Derewenda ZS]] |
| - | [[Category: Derewenda | + | [[Category: Swenson L]] |
| - | [[Category: Swenson | + | [[Category: Wei Y]] |
| - | [[Category: Wei | + | [[Category: Yamaguchi S]] |
| - | [[Category: Yamaguchi | + | |
Current revision
AN UNUSUAL BURIED POLAR CLUSTER IN A FAMILY OF FUNGAL LIPASES
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