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1n2a

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[[Image:1n2a.jpg|left|200px]]
 
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==Crystal Structure of a Bacterial Glutathione Transferase from Escherichia coli with Glutathione Sulfonate in the Active Site==
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The line below this paragraph, containing "STRUCTURE_1n2a", creates the "Structure Box" on the page.
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<StructureSection load='1n2a' size='340' side='right'caption='[[1n2a]], [[Resolution|resolution]] 1.90&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'>[[1n2a]] 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=1N2A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N2A 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]] 1.9&#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=GTS:GLUTATHIONE+SULFONIC+ACID'>GTS</scene></td></tr>
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{{STRUCTURE_1n2a| PDB=1n2a | 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=1n2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n2a OCA], [https://pdbe.org/1n2a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n2a RCSB], [https://www.ebi.ac.uk/pdbsum/1n2a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n2a ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GSTA_ECOLI GSTA_ECOLI] Catalyzes the conjugation of reduced glutathione (GSH) to a wide number of exogenous and endogenous hydrophobic electrophiles. Shows activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and ethacrynic acid. Also possesses thiol:disulfide oxidoreductase activity, using GSH to reduce bis-(2-hydroxyethyl) disulfide (HEDS). Has a low level of glutathione-dependent peroxidase activity toward cumene hydroperoxide. Is important for defense against oxidative stress, probably via its peroxidase activity.<ref>PMID:7798255</ref> <ref>PMID:2185038</ref> <ref>PMID:17018556</ref> <ref>PMID:18778244</ref>
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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/n2/1n2a_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=1n2a ConSurf].
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<div style="clear:both"></div>
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'''Crystal Structure of a Bacterial Glutathione Transferase from Escherichia coli with Glutathione Sulfonate in the Active Site'''
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==See Also==
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*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
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== References ==
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==Overview==
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<references/>
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Multiple sequence alignments of the eight glutathione (GSH) transferase homologues encoded in the genome of Escherichia coli were used to define a consensus sequence for the proteins. The consensus sequence was analyzed in the context of the three-dimensional structure of the gst gene product (EGST) obtained from two different crystal forms of the enzyme. The enzyme consists of two domains. The N-terminal region (domain I) has a thioredoxin-like alpha/beta-fold, while the C-terminal domain (domain II) is all alpha-helical. The majority of the consensus residues (12/17) reside in the N-terminal domain. Fifteen of the 17 residues are involved in hydrophobic core interactions, turns, or electrostatic interactions between the two domains. The results suggest that all of the homologues retain a well-defined group of structural elements both in and between the N-terminal alpha/beta domain and the C-terminal domain. The conservation of two key residues for the recognition motif for the gamma-glutamyl-portion of GSH indicates that the homologues may interact with GSH or GSH analogues such as glutathionylspermidine or alpha-amino acids. The genome context of two of the homologues forms the basis for a hypothesis that the b2989 and yibF gene products are involved in glutathionylspermidine and selenium biochemistry, respectively.
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__TOC__
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</StructureSection>
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==About this Structure==
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1N2A is a [[Single protein]] 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=1N2A OCA].
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==Reference==
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Conserved structural elements in glutathione transferase homologues encoded in the genome of Escherichia coli., Rife CL, Parsons JF, Xiao G, Gilliland GL, Armstrong RN, Proteins. 2003 Dec 1;53(4):777-82. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14635120 14635120]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Glutathione transferase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Armstrong RN]]
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[[Category: Armstrong, R N.]]
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[[Category: Gilliland GL]]
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[[Category: Gilliland, G L.]]
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[[Category: Parsons JF]]
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[[Category: Parsons, J F.]]
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[[Category: Rife CL]]
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[[Category: Rife, C L.]]
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[[Category: Xiao G]]
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[[Category: Xiao, G.]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:00:02 2008''
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Current revision

Crystal Structure of a Bacterial Glutathione Transferase from Escherichia coli with Glutathione Sulfonate in the Active Site

PDB ID 1n2a

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