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| | ==E. coli Thioesterase I/Protease I/Lysophospholipase L1 in complexed with diethyl phosphono moiety== | | ==E. coli Thioesterase I/Protease I/Lysophospholipase L1 in complexed with diethyl phosphono moiety== |
| - | <StructureSection load='1j00' size='340' side='right' caption='[[1j00]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='1j00' size='340' side='right'caption='[[1j00]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1j00]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J00 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1J00 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1j00]] 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=1J00 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J00 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SDP:2-AMINO-3-(DIETHOXY-PHOSPHORYLOXY)-PROPIONIC+ACID'>SDP</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SDP:2-AMINO-3-(DIETHOXY-PHOSPHORYLOXY)-PROPIONIC+ACID'>SDP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jrl|1jrl]], [[1ivn|1ivn]]</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=1j00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j00 OCA], [https://pdbe.org/1j00 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j00 RCSB], [https://www.ebi.ac.uk/pdbsum/1j00 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j00 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tesA/apeA/pldC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j00 OCA], [http://pdbe.org/1j00 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1j00 RCSB], [http://www.ebi.ac.uk/pdbsum/1j00 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1j00 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TESA_ECOLI TESA_ECOLI]] Hydrolyzes only long chain acyl thioesters (C12-C18). Specificity similar to chymotrypsin. | + | [https://www.uniprot.org/uniprot/TESA_ECOLI TESA_ECOLI] Hydrolyzes only long chain acyl thioesters (C12-C18). Specificity similar to chymotrypsin. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1j00" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1j00" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Thioesterase 3D structures|Thioesterase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: Liaw, Y C]] | + | [[Category: Large Structures]] |
| - | [[Category: Lo, Y C]] | + | [[Category: Liaw Y-C]] |
| - | [[Category: Shaw, J F]] | + | [[Category: Lo Y-C]] |
| - | [[Category: Hydrolase]]
| + | [[Category: Shaw J-F]] |
| - | [[Category: Protease]]
| + | |
| Structural highlights
Function
TESA_ECOLI Hydrolyzes only long chain acyl thioesters (C12-C18). Specificity similar to chymotrypsin.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lo YC, Lin SC, Shaw JF, Liaw YC. 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. J Mol Biol. 2003 Jul 11;330(3):539-51. PMID:12842470
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