2fs2

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(New page: 200px<br /><applet load="2fs2" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fs2, resolution 2.000&Aring;" /> '''Structure of the E....)
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[[Image:2fs2.gif|left|200px]]<br /><applet load="2fs2" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2fs2, resolution 2.000&Aring;" />
 
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'''Structure of the E. coli PaaI protein from the phyenylacetic acid degradation operon'''<br />
 
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==Overview==
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==Structure of the E. coli PaaI protein from the phyenylacetic acid degradation operon==
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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.
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<StructureSection load='2fs2' size='340' side='right'caption='[[2fs2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FS2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FS2 FirstGlance]. <br>
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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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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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=2fs2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fs2 OCA], [https://pdbe.org/2fs2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fs2 RCSB], [https://www.ebi.ac.uk/pdbsum/2fs2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fs2 ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/2fs2 TOPSAN]</span></td></tr>
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</table>
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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/fs/2fs2_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2fs2 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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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.
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==About this Structure==
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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<ref>PMID:16464851</ref>
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2FS2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FS2 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16464851 16464851]
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</div>
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[[Category: Escherichia coli]]
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<div class="pdbe-citations 2fs2" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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== References ==
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[[Category: Buglino, J.A.]]
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<references/>
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[[Category: Burley, S.K.]]
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__TOC__
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[[Category: Kniewel, R.]]
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</StructureSection>
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[[Category: Lima, C.D.]]
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[[Category: Large Structures]]
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[[Category: NYSGXRC, New.York.Structural.GenomiX.Research.Consortium.]]
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[[Category: Buglino JA]]
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[[Category: Solorzano, V.]]
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[[Category: Burley SK]]
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[[Category: Wu, J.]]
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[[Category: Kniewel R]]
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[[Category: SO4]]
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[[Category: Lima CD]]
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[[Category: degradation]]
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[[Category: Solorzano V]]
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[[Category: new york structural genomix research consortium]]
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[[Category: Wu J]]
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[[Category: nysgxrc]]
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[[Category: operon]]
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[[Category: phenylacetic acid]]
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[[Category: protein structure initiative]]
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[[Category: psi]]
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[[Category: structural genomics]]
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[[Category: t820]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:43:55 2007''
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Current revision

Structure of the E. coli PaaI protein from the phyenylacetic acid degradation operon

PDB ID 2fs2

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