1jrl

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{{Seed}}
 
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[[Image:1jrl.png|left|200px]]
 
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==Crystal structure of E. coli Lysophospholiase L1/Acyl-CoA Thioesterase I/Protease I L109P mutant==
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The line below this paragraph, containing "STRUCTURE_1jrl", creates the "Structure Box" on the page.
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<StructureSection load='1jrl' size='340' side='right'caption='[[1jrl]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1jrl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JRL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JRL FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.95&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1jrl| PDB=1jrl | SCENE= }}
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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=1jrl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jrl OCA], [https://pdbe.org/1jrl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jrl RCSB], [https://www.ebi.ac.uk/pdbsum/1jrl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jrl ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TESA_ECOLI TESA_ECOLI] Hydrolyzes only long chain acyl thioesters (C12-C18). Specificity similar to chymotrypsin.
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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/jr/1jrl_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=1jrl 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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Escherichia coli thioesterase I (TAP) is a multifunctional enzyme possessing activities of thioesterase, esterase, arylesterase, protease, and lysophospholipase. In particular, TAP has stereoselectivity for amino acid derivative substrates, hence it is useful for the kinetic resolution of racemic mixtures of industrial chemicals. In the present work, the crystal structure of native TAP was determined at 1.9A, revealing a minimal SGNH-hydrolase fold. The structure of TAP in complex with a diethyl phosphono moiety (DEP) identified its catalytic triad, Ser10-Asp154-His157, and oxyanion hole, Ser10-Gly44-Asn73. The oxyanion hole of TAP consists of three residues each separated from the other by more than 3.5A, implying that all of them are highly polarized when substrate bound. The catalytic (His)C(epsilon1)-H...O=C hydrogen bond usually plays a role in the catalytic mechanisms of most serine hydrolases, however, there were none present in SGNH-hydrolases. We propose that the existence of the highly polarized tri-residue-constituted oxyanion hole compensates for the lack of a (His)C(epsilon1)-H...O=C hydrogen bond. This suggests that members of the SGNH-hydrolase family may employ a unique catalytic mechanism. In addition, most SGNH-hydrolases have low sequence identities and presently there is no clear criterion to define consensus sequence blocks. Through comparison of TAP and the three SGNH-hydrolase structures currently known, we have identified a unique hydrogen bond network which stabilizes the catalytic center: a newly discovered structural feature of SGNH-hydrolases. We have defined these consensus sequence blocks providing a basis for the sub-classification of SGNH-hydrolases.
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===Crystal structure of E. coli Lysophospholiase L1/Acyl-CoA Thioesterase I/Protease I L109P mutant===
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Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network.,Lo YC, Lin SC, Shaw JF, Liaw YC J Mol Biol. 2003 Jul 11;330(3):539-51. PMID:12842470<ref>PMID:12842470</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 1jrl" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_12842470}}, adds the Publication Abstract to the page
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*[[Thioesterase 3D structures|Thioesterase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 12842470 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12842470}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1JRL is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JRL OCA].
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==Reference==
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<ref group="xtra">PMID:12842470</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Liaw, Y C.]]
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[[Category: Large Structures]]
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[[Category: Lin, S C.]]
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[[Category: Liaw Y-C]]
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[[Category: Lo, Y C.]]
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[[Category: Lin S-C]]
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[[Category: Shaw, J F.]]
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[[Category: Lo Y-C]]
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[[Category: Hydrolase]]
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[[Category: Shaw J-F]]
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[[Category: Protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 20:24:45 2009''
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Current revision

Crystal structure of E. coli Lysophospholiase L1/Acyl-CoA Thioesterase I/Protease I L109P mutant

PDB ID 1jrl

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