1tia

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Current revision (08:39, 14 February 2024) (edit) (undo)
 
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<StructureSection load='1tia' size='340' side='right'caption='[[1tia]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='1tia' size='340' side='right'caption='[[1tia]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1tia]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Penca Penca]. 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>
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<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>
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</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>
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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]] 2.1&#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=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>
<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 ==
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[[https://www.uniprot.org/uniprot/MDLA_PENCA MDLA_PENCA]] Hydrolyzes mono- and diacylglycerol but not triacylglycerol.
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[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]]
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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=1tia 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=1tia ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1tia" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Lipase 3D Structures|Lipase 3D Structures]]
*[[Lipase 3D Structures|Lipase 3D Structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Penca]]
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[[Category: Penicillium camemberti]]
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[[Category: Triacylglycerol lipase]]
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[[Category: Derewenda U]]
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[[Category: Derewenda, U]]
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[[Category: Derewenda ZS]]
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[[Category: Derewenda, Z S]]
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[[Category: Swenson L]]
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[[Category: Swenson, L]]
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[[Category: Wei Y]]
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[[Category: Wei, Y]]
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[[Category: Yamaguchi S]]
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[[Category: Yamaguchi, S]]
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Current revision

AN UNUSUAL BURIED POLAR CLUSTER IN A FAMILY OF FUNGAL LIPASES

PDB ID 1tia

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