2hih

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[[Image:2hih.jpg|left|200px]]<br /><applet load="2hih" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2hih, resolution 2.860&Aring;" />
 
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'''Crystal structure of Staphylococcus hyicus lipase'''<br />
 
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==About this Structure==
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==Crystal structure of Staphylococcus hyicus lipase==
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2HIH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_hyicus Staphylococcus hyicus] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HIH OCA].
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<StructureSection load='2hih' size='340' side='right'caption='[[2hih]], [[Resolution|resolution]] 2.86&Aring;' scene=''>
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[[Category: Single protein]]
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== Structural highlights ==
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[[Category: Staphylococcus hyicus]]
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<table><tr><td colspan='2'>[[2hih]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_hyicus Staphylococcus hyicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HIH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HIH FirstGlance]. <br>
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[[Category: Triacylglycerol lipase]]
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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]] 2.86&#8491;</td></tr>
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[[Category: Dijkstra, B W.]]
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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=ZN:ZINC+ION'>ZN</scene></td></tr>
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[[Category: Nardini, M.]]
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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=2hih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hih OCA], [https://pdbe.org/2hih PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hih RCSB], [https://www.ebi.ac.uk/pdbsum/2hih PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hih ProSAT]</span></td></tr>
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[[Category: Pouderoyen, G van.]]
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</table>
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[[Category: Tiesinga, J J.W.]]
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== Function ==
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[[Category: CA]]
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[https://www.uniprot.org/uniprot/LIP_STAHY LIP_STAHY]
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[[Category: ZN]]
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== Evolutionary Conservation ==
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[[Category: a1 phospholipase]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: lipase]]
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Check<jmol>
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[[Category: phospholipid binding]]
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hi/2hih_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=2hih 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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Staphylococcus hyicus lipase differs from other bacterial lipases in its high phospholipase A1 activity. Here, we present the crystal structure of the S. hyicus lipase at 2.86 A resolution. The lipase is in an open conformation, with the active site partly covered by a neighbouring molecule. Ser124, Asp314 and His355 form the catalytic triad. The substrate-binding cavity contains two large hydrophobic acyl chain-binding pockets and a shallow and more polar third pocket that is capable of binding either a (short) fatty acid or a phospholipid head-group. A model of a phospholipid bound in the active site shows that Lys295 is at hydrogen bonding distance from the substrate's phosphate group. Residues Ser356, Glu292 and Thr294 hold the lysine in position by hydrogen bonding and electrostatic interactions. These observations explain the biochemical data showing the importance of Lys295 and Ser356 for phospholipid binding and phospholipase A1 activity.
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:42:14 2008''
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Structural basis of phospholipase activity of Staphylococcus hyicus lipase.,Tiesinga JJ, van Pouderoyen G, Nardini M, Ransac S, Dijkstra BW J Mol Biol. 2007 Aug 10;371(2):447-56. Epub 2007 May 21. PMID:17582438<ref>PMID:17582438</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 2hih" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Lipase 3D Structures|Lipase 3D Structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Staphylococcus hyicus]]
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[[Category: Dijkstra BW]]
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[[Category: Nardini M]]
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[[Category: Tiesinga JJW]]
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[[Category: Van Pouderoyen G]]

Current revision

Crystal structure of Staphylococcus hyicus lipase

PDB ID 2hih

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