3e4d
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3e4d is ON HOLD Authors: Van Straaten, K.E., Gonzalez, C.F., Valladares, R.B., Xu, X., Savchenko, A.V., Sanders, D.A.R. Description: Structural and...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structural and Kinetic Study of an S-Formylglutathione Hydrolase from Agrobacterium tumefaciens== | |
| + | <StructureSection load='3e4d' size='340' side='right'caption='[[3e4d]], [[Resolution|resolution]] 2.01Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3e4d]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Agrobacterium_fabrum_str._C58 Agrobacterium fabrum str. C58]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E4D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E4D FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.01Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=3e4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e4d OCA], [https://pdbe.org/3e4d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e4d RCSB], [https://www.ebi.ac.uk/pdbsum/3e4d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e4d ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A9CJ11_AGRFC A9CJ11_AGRFC] Serine hydrolase involved in the detoxification of formaldehyde.[RuleBase:RU363068] | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e4/3e4d_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=3e4d ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The structure of the Atu1476 protein from Agrobacterium tumefaciens was determined at 2 A resolution. The crystal structure and biochemical characterization of this enzyme support the conclusion that this protein is an S-formylglutathione hydrolase (AtuSFGH). The three dimensional structure of AtuSFGH contains the alpha/beta hydrolase fold topology and exists as a homo-dimer. Contacts between the two monomers in the dimer are formed both by hydrogen bonds and salt bridges. Biochemical characterization reveals that AtuSFGH hydrolyzes C-O bonds with high affinity towards short to medium chain esters, unlike the other known SFGHs which have greater affinity towards shorter chained esters. A potential role for Cys54 in regulation of enzyme activity through S-glutathionylation is also proposed. | ||
| - | + | The structure of a putative S-formylglutathione hydrolase from agrobacterium tumefaciens.,van Straaten KE, Gonzalez CF, Valladares RB, Xu X, Savchenko AV, Sanders DA Protein Sci. 2009 Aug 3. PMID:19653299<ref>PMID:19653299</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3e4d" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Agrobacterium fabrum str. C58]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Gonzalez CF]] | ||
| + | [[Category: Sanders DAR]] | ||
| + | [[Category: Savchenko AV]] | ||
| + | [[Category: Valladares RB]] | ||
| + | [[Category: Van Straaten KE]] | ||
| + | [[Category: Xu X]] | ||
Current revision
Structural and Kinetic Study of an S-Formylglutathione Hydrolase from Agrobacterium tumefaciens
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