1n2a

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Revision as of 10:17, 25 October 2017

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

Structural highlights

1n2a is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	GT_1787923 ("Bacillus coli" Migula 1895)
Activity:	Glutathione transferase, with EC number 2.5.1.18
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2] ^[3] ^[4]

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

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.

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:14635120^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Nishida M, Kong KH, Inoue H, Takahashi K. Molecular cloning and site-directed mutagenesis of glutathione S-transferase from Escherichia coli. The conserved tyrosyl residue near the N terminus is not essential for catalysis. J Biol Chem. 1994 Dec 23;269(51):32536-41. PMID:7798255
↑ Arca P, Garcia P, Hardisson C, Suarez JE. Purification and study of a bacterial glutathione S-transferase. FEBS Lett. 1990 Apr 9;263(1):77-9. PMID:2185038
↑ Kanai T, Takahashi K, Inoue H. Three distinct-type glutathione S-transferases from Escherichia coli important for defense against oxidative stress. J Biochem. 2006 Nov;140(5):703-11. Epub 2006 Oct 3. PMID:17018556 doi:http://dx.doi.org/10.1093/jb/mvj199
↑ Wang XY, Zhang ZR, Perrett S. Characterization of the activity and folding of the glutathione transferase from Escherichia coli and the roles of residues Cys(10) and His(106). Biochem J. 2009 Jan 1;417(1):55-64. doi: 10.1042/BJ20071702. PMID:18778244 doi:http://dx.doi.org/10.1042/BJ20071702
↑ Rife CL, Parsons JF, Xiao G, Gilliland GL, Armstrong RN. Conserved structural elements in glutathione transferase homologues encoded in the genome of Escherichia coli. Proteins. 2003 Dec 1;53(4):777-82. PMID:14635120 doi:10.1002/prot.10452

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1n2a"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of a Bacterial Glutathione Transferase from Escherichia coli with Glutathione Sulfonate in the Active Site==
 <StructureSection load='1n2a' size='340' side='right' caption='[[1n2a]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GT_1787923 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n2a OCA], [http://pdbe.org/1n2a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n2a RCSB], [http://www.ebi.ac.uk/pdbsum/1n2a PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n2a OCA], [http://pdbe.org/1n2a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n2a RCSB], [http://www.ebi.ac.uk/pdbsum/1n2a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1n2a ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
     <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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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>
 <div style="background-color:#fffaf0;">
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 1n2a" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Glutathione S-transferase|Glutathione S-transferase]]
 == References ==
 <references/>

1n2a

From Proteopedia

Revision as of 10:17, 25 October 2017

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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