1ku0

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[[Image:1ku0.jpg|left|200px]]
 
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{{Structure
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==Structure of the Bacillus stearothermophilus L1 lipase==
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|PDB= 1ku0 |SIZE=350|CAPTION= <scene name='initialview01'>1ku0</scene>, resolution 2.0&Aring;
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<StructureSection load='1ku0' size='340' side='right'caption='[[1ku0]], [[Resolution|resolution]] 2.00&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=ZN:ZINC+ION'>ZN</scene>
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<table><tr><td colspan='2'>[[1ku0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KU0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KU0 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]] 2&#8491;</td></tr>
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|GENE=
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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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|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=1ku0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ku0 OCA], [https://pdbe.org/1ku0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ku0 RCSB], [https://www.ebi.ac.uk/pdbsum/1ku0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ku0 ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ku0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ku0 OCA], [http://www.ebi.ac.uk/pdbsum/1ku0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ku0 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/O66015_GEOSE O66015_GEOSE]
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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/ku/1ku0_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=1ku0 ConSurf].
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<div style="clear:both"></div>
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'''Structure of the Bacillus stearothermophilus L1 lipase'''
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==See Also==
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*[[Lipase 3D Structures|Lipase 3D Structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The bacterial thermoalkalophilic lipases optimally hydrolyze saturated fatty acids at elevated temperatures. They also have significant sequence homology with staphylococcal lipases, and both the thermoalkalophilic and staphylococcal lipases are grouped as the lipase family I.5. We report here the first crystal structure of the lipase family I.5, the structure of a thermoalkalophilic lipase from Bacillus stearothermophilus L1 (L1 lipase) determined at 2.0-A resolution. The structure is in a closed conformation, and the active site is buried under a long lid helix. Unexpectedly, the structure exhibits a zinc-binding site in an extra domain that accounts for the larger molecular size of the family I.5 enzymes in comparison to other microbial lipases. The zinc-coordinated extra domain makes tight interactions with the loop extended from the C terminus of the lid helix, suggesting that the activation of the family I.5 lipases may be regulated by the strength of the interactions. The unusually long lid helix makes strong hydrophobic interactions with its neighbors. The structural information together with previous biochemical observations indicate that the temperature-mediated lid opening is triggered by the thermal dissociation of the hydrophobic interactions.
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==About this Structure==
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1KU0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KU0 OCA].
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==Reference==
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Novel zinc-binding center and a temperature switch in the Bacillus stearothermophilus L1 lipase., Jeong ST, Kim HK, Kim SJ, Chi SW, Pan JG, Oh TK, Ryu SE, J Biol Chem. 2002 May 10;277(19):17041-7. Epub 2002 Feb 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11859083 11859083]
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[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Triacylglycerol lipase]]
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[[Category: Chi S-W]]
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[[Category: Chi, S W.]]
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[[Category: Jeong S-T]]
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[[Category: Jeong, S T.]]
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[[Category: Kim H-K]]
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[[Category: Kim, H K.]]
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[[Category: Kim S-J]]
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[[Category: Kim, S J.]]
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[[Category: Oh T-K]]
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[[Category: Oh, T K.]]
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[[Category: Pan J-G]]
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[[Category: Pan, J G.]]
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[[Category: Ryu S-E]]
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[[Category: Ryu, S E.]]
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[[Category: hydrolase]]
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[[Category: lipase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:53:38 2008''
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Current revision

Structure of the Bacillus stearothermophilus L1 lipase

PDB ID 1ku0

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