1n2a: Difference between revisions

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-[[Image:1n2a.jpg|left|200px]]
- {{Structure
+==Crystal Structure of a Bacterial Glutathione Transferase from Escherichia coli with Glutathione Sulfonate in the Active Site==
-|PDB= 1n2a |SIZE=350|CAPTION= <scene name='initialview01'>1n2a</scene>, resolution 1.90&Aring;
+<StructureSection load='1n2a' size='340' side='right'caption='[[1n2a]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=GTS:GLUTATHIONE SULFONIC ACID'>GTS</scene>
+<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>
-|ACTIVITY= [http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18]
+</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>
-|GENE= GT_1787923 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
+<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>
-}}
+<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>
+</table>
+== Function ==
+[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>
+== 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/n2/1n2a_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1n2a ConSurf].
+<div style="clear:both"></div>
-'''Crystal Structure of a Bacterial Glutathione Transferase from Escherichia coli with Glutathione Sulfonate in the Active Site'''
+==See Also==
+*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
+== References ==
-==Overview==
+<references/>
-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.
+__TOC__
+</StructureSection>
-==About this Structure==
-N2A 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].
-==Reference==
-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]
 [[Category: Escherichia coli]]
-[[Category: Glutathione transferase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Armstrong RN]]
-[[Category: Armstrong, R N.]]
+[[Category: Gilliland GL]]
-[[Category: Gilliland, G L.]]
+[[Category: Parsons JF]]
-[[Category: Parsons, J F.]]
+[[Category: Rife CL]]
-[[Category: Rife, C L.]]
+[[Category: Xiao G]]
-[[Category: Xiao, G.]]
-[[Category: GTS]]
-[[Category: transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:51:13 2008''