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| | <StructureSection load='1psu' size='340' side='right'caption='[[1psu]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='1psu' size='340' side='right'caption='[[1psu]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1psu]] is a 2 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=1PSU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1PSU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1psu]] is a 2 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=1PSU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PSU FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 2.2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PAAI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1psu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1psu OCA], [http://pdbe.org/1psu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1psu RCSB], [http://www.ebi.ac.uk/pdbsum/1psu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1psu ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/1psu TOPSAN]</span></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=1psu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1psu OCA], [https://pdbe.org/1psu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1psu RCSB], [https://www.ebi.ac.uk/pdbsum/1psu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1psu ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/1psu TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PAAI_ECOLI PAAI_ECOLI]] Thioesterase with a preference for ring-hydroxylated phenylacetyl-CoA esters. Hydrolyzes 3,4-dihydroxyphenylacetyl-CoA, 3-hydroxyphenylacetyl-CoA and 4-hydroxyphenylacetyl-CoA. Inactive towards 4-hydroxybenzoyl-CoA and 4-hydroxyphenacyl-CoA.<ref>PMID:9748275</ref> <ref>PMID:16464851</ref> | + | [https://www.uniprot.org/uniprot/PAAI_ECOLI PAAI_ECOLI] Thioesterase with a preference for ring-hydroxylated phenylacetyl-CoA esters. Hydrolyzes 3,4-dihydroxyphenylacetyl-CoA, 3-hydroxyphenylacetyl-CoA and 4-hydroxyphenylacetyl-CoA. Inactive towards 4-hydroxybenzoyl-CoA and 4-hydroxyphenacyl-CoA.<ref>PMID:9748275</ref> <ref>PMID:16464851</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ps/1psu_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ps/1psu_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Buglino, J]] | + | [[Category: Buglino J]] |
| - | [[Category: Burley, S K]] | + | [[Category: Burley SK]] |
| - | [[Category: Kniewel, R]] | + | [[Category: Kniewel R]] |
| - | [[Category: Lima, C D]] | + | [[Category: Lima CD]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Solorzano V]] |
| - | [[Category: Solorzano, V]] | + | [[Category: Wu J]] |
| - | [[Category: Wu, J]] | + | |
| - | [[Category: Degradation]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: NYSGXRC, New York SGX Research Center for Structural Genomics]]
| + | |
| - | [[Category: Operon]]
| + | |
| - | [[Category: Phenylacetic acid]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| - | [[Category: T820]]
| + | |
| Structural highlights
Function
PAAI_ECOLI Thioesterase with a preference for ring-hydroxylated phenylacetyl-CoA esters. Hydrolyzes 3,4-dihydroxyphenylacetyl-CoA, 3-hydroxyphenylacetyl-CoA and 4-hydroxyphenylacetyl-CoA. Inactive towards 4-hydroxybenzoyl-CoA and 4-hydroxyphenacyl-CoA.[1] [2]
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
The structure and biochemical function of the hot dog-fold thioesterase PaaI operative in the aerobic phenylacetate degradation pathway are examined. PaaI showed modest activity with phenylacetyl-coenzyme A, suggestive of a role in coenzyme A release from this pathway intermediate in the event of limiting downstream pathway enzymes. Minimal activity was observed with aliphatic acyl-coenzyme A thioesters, which ruled out PaaI function in the lower phenylacetate pathway. PaaI was most active with ring-hydroxylated phenylacetyl-coenzyme A thioesters. The x-ray crystal structure of the Escherichia coli thioesterase is reported and analyzed to define the structural basis of substrate recognition and catalysis. The contributions of catalytic and substrate binding residues, thus, identified were examined through steady-state kinetic analysis of site-directed mutant proteins.
Structure, function, and mechanism of the phenylacetate pathway hot dog-fold thioesterase PaaI.,Song F, Zhuang Z, Finci L, Dunaway-Mariano D, Kniewel R, Buglino JA, Solorzano V, Wu J, Lima CD J Biol Chem. 2006 Apr 21;281(16):11028-38. Epub 2006 Feb 7. PMID:16464851[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ferrandez A, Minambres B, Garcia B, Olivera ER, Luengo JM, Garcia JL, Diaz E. Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway. J Biol Chem. 1998 Oct 2;273(40):25974-86. PMID:9748275
- ↑ Song F, Zhuang Z, Finci L, Dunaway-Mariano D, Kniewel R, Buglino JA, Solorzano V, Wu J, Lima CD. Structure, function, and mechanism of the phenylacetate pathway hot dog-fold thioesterase PaaI. J Biol Chem. 2006 Apr 21;281(16):11028-38. Epub 2006 Feb 7. PMID:16464851 doi:http://dx.doi.org/10.1074/jbc.M513896200
- ↑ Song F, Zhuang Z, Finci L, Dunaway-Mariano D, Kniewel R, Buglino JA, Solorzano V, Wu J, Lima CD. Structure, function, and mechanism of the phenylacetate pathway hot dog-fold thioesterase PaaI. J Biol Chem. 2006 Apr 21;281(16):11028-38. Epub 2006 Feb 7. PMID:16464851 doi:http://dx.doi.org/10.1074/jbc.M513896200
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