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2es4

From Proteopedia

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[[Image:2es4.gif|left|200px]]
 
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{{Structure
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==Crystal structure of the Burkholderia glumae lipase-specific foldase in complex with its cognate lipase==
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|PDB= 2es4 |SIZE=350|CAPTION= <scene name='initialview01'>2es4</scene>, resolution 1.85&Aring;
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<StructureSection load='2es4' size='340' side='right'caption='[[2es4]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>
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<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>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </span>
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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]] 1.85&#8491;</td></tr>
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|GENE= lifO, lipB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=337 Burkholderia glumae])
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<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>
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|DOMAIN=
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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=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>
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|RELATEDENTRY=[[1cvl|1CVL]], [[1tah|1TAH]], [[1qge|1QGE]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2es4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2es4 OCA], [http://www.ebi.ac.uk/pdbsum/2es4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2es4 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/LIP_BURPL LIP_BURPL] Catalyzes the hydrolysis of triacylglycerol.<ref>PMID:1476423</ref> <ref>PMID:7786905</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/es/2es4_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2es4 ConSurf].
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<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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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.
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'''Crystal structure of the Burkholderia glumae lipase-specific foldase in complex with its cognate lipase'''
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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>
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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 2es4" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Lipase 3D Structures|Lipase 3D Structures]]
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== References ==
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==About this Structure==
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<references/>
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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].
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__TOC__
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</StructureSection>
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==Reference==
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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]
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[[Category: Burkholderia glumae]]
[[Category: Burkholderia glumae]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Triacylglycerol lipase]]
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[[Category: Pauwels K]]
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[[Category: Gelder, P Van.]]
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[[Category: Savvides SN]]
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[[Category: Pauwels, K.]]
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[[Category: Tommassen J]]
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[[Category: Savvides, S N.]]
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[[Category: Van Gelder P]]
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[[Category: Tommassen, J.]]
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[[Category: Wyns L]]
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[[Category: Wyns, L.]]
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[[Category: a/b hydrolase fold]]
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[[Category: all alpha helix protein]]
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[[Category: extensive interaction area]]
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[[Category: protein-protein complex]]
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[[Category: steric chaperone]]
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[[Category: triacylglycerol hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:53:04 2008''
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Current revision

Crystal structure of the Burkholderia glumae lipase-specific foldase in complex with its cognate lipase

PDB ID 2es4

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