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[[Image:2es4.gif|left|200px]]
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{{STRUCTURE_2es4|  PDB=2es4  |  SCENE=  }}
'''Crystal structure of the Burkholderia glumae lipase-specific foldase in complex with its cognate lipase'''


==Crystal structure of the Burkholderia glumae lipase-specific foldase in complex with its cognate lipase==
<StructureSection load='2es4' size='340' side='right'caption='[[2es4]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2es4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_glumae Burkholderia glumae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ES4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ES4 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></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=2es4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2es4 OCA], [https://pdbe.org/2es4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2es4 RCSB], [https://www.ebi.ac.uk/pdbsum/2es4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2es4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LIP_BURPL LIP_BURPL] Catalyzes the hydrolysis of triacylglycerol.<ref>PMID:1476423</ref> <ref>PMID:7786905</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/es/2es4_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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/main_output.php?pdb_ID=2es4 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Secretion via the type II secretion pathway in Gram-negative bacteria often relies crucially on steric chaperones in the periplasm. Here, we report the crystal structure of the soluble form of a lipase-specific foldase (Lif) from Burkholderia glumae in complex with its cognate lipase. The structure reveals how Lif uses a novel alpha-helical scaffold to embrace lipase, thereby creating an unusually extensive folding platform.


==Overview==
Structure of a membrane-based steric chaperone in complex with its lipase substrate.,Pauwels K, Lustig A, Wyns L, Tommassen J, Savvides SN, Van Gelder P Nat Struct Mol Biol. 2006 Apr;13(4):374-5. Epub 2006 Mar 5. PMID:16518399<ref>PMID:16518399</ref>
Secretion via the type II secretion pathway in Gram-negative bacteria often relies crucially on steric chaperones in the periplasm. Here, we report the crystal structure of the soluble form of a lipase-specific foldase (Lif) from Burkholderia glumae in complex with its cognate lipase. The structure reveals how Lif uses a novel alpha-helical scaffold to embrace lipase, thereby creating an unusually extensive folding platform.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2ES4 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Burkholderia_glumae Burkholderia glumae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ES4 OCA].
</div>
<div class="pdbe-citations 2es4" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structure of a membrane-based steric chaperone in complex with its lipase substrate., Pauwels K, Lustig A, Wyns L, Tommassen J, Savvides SN, Van Gelder P, Nat Struct Mol Biol. 2006 Apr;13(4):374-5. Epub 2006 Mar 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16518399 16518399]
*[[Lipase 3D Structures|Lipase 3D Structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Burkholderia glumae]]
[[Category: Burkholderia glumae]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Triacylglycerol lipase]]
[[Category: Pauwels K]]
[[Category: Gelder, P Van.]]
[[Category: Savvides SN]]
[[Category: Pauwels, K.]]
[[Category: Tommassen J]]
[[Category: Savvides, S N.]]
[[Category: Van Gelder P]]
[[Category: Tommassen, J.]]
[[Category: Wyns L]]
[[Category: Wyns, L.]]
[[Category: A/b hydrolase fold]]
[[Category: All alpha helix protein]]
[[Category: Extensive interaction area]]
[[Category: Protein-protein complex]]
[[Category: Steric chaperone]]
[[Category: Triacylglycerol hydrolase]]
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Retrieved from "https://proteopedia.org/2es4"