|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of Salmonella thyphimurium LT2 glyoxalase II== | | ==Crystal structure of Salmonella thyphimurium LT2 glyoxalase II== |
| - | <StructureSection load='2qed' size='340' side='right' caption='[[2qed]], [[Resolution|resolution]] 1.45Å' scene=''> | + | <StructureSection load='2qed' size='340' side='right'caption='[[2qed]], [[Resolution|resolution]] 1.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2qed]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Salty Salty]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2obw 2obw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QED OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2QED FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2qed]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salty Salty]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2obw 2obw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QED OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QED FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gloB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=99287 SALTY])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gloB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=99287 SALTY])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.6 3.1.2.6] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.6 3.1.2.6] </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=2qed FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qed OCA], [http://pdbe.org/2qed PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qed RCSB], [http://www.ebi.ac.uk/pdbsum/2qed PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2qed ProSAT]</span></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=2qed FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qed OCA], [https://pdbe.org/2qed PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qed RCSB], [https://www.ebi.ac.uk/pdbsum/2qed PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qed ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GLO2_SALTY GLO2_SALTY]] Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid. | + | [[https://www.uniprot.org/uniprot/GLO2_SALTY GLO2_SALTY]] Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 35: |
Line 35: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Salty]] | | [[Category: Salty]] |
| | [[Category: Bermudez, V A.Campos]] | | [[Category: Bermudez, V A.Campos]] |
| Structural highlights
Function
[GLO2_SALTY] Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
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
Glyoxalase II is a hydrolytic enzyme part of the glyoxalase system, responsible for detoxifying several cytotoxic compounds employing glutathione. Glyoxalase II belongs to the superfamily of metallo-beta-lactamases, with a conserved motif able to bind up to two metal ions in their active sites, generally zinc. Instead, several eukaryotic glyoxalases II have been characterized with different ratios of iron, zinc, and manganese ions. We have expressed a gene coding for a putative member of this enzyme superfamily from Salmonella typhimurium that we demonstrate, on the basis of its activity, to be a glyoxalase II, named GloB. Recombinant GloB expressed in Escherichia coli was purified with variable amounts of iron, zinc, and manganese. All forms display similar activities, as can be shown from protein expression in minimal medium supplemented with specific metal ions. The crystal structure of GloB solved at 1.4 A shows a protein fold and active site similar to those of its eukaryotic homologues. NMR and EPR experiments also reveal a conserved electronic structure at the metal site. GloB is therefore able to accommodate these different metal ions and to carry out the hydrolytic reaction with similar efficiencies in all cases. The metal promiscuity of this enzyme (in contrast to other members of the same superfamily) can be accounted for by the presence of a conserved Asp residue acting as a second-shell ligand that is expected to increase the hardness of the metal binding site, therefore favoring iron uptake in glyoxalases II.
Biochemical and structural characterization of Salmonella typhimurium glyoxalase II: new insights into metal ion selectivity.,Campos-Bermudez VA, Leite NR, Krog R, Costa-Filho AJ, Soncini FC, Oliva G, Vila AJ Biochemistry. 2007 Oct 2;46(39):11069-79. Epub 2007 Sep 1. PMID:17764159[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Campos-Bermudez VA, Leite NR, Krog R, Costa-Filho AJ, Soncini FC, Oliva G, Vila AJ. Biochemical and structural characterization of Salmonella typhimurium glyoxalase II: new insights into metal ion selectivity. Biochemistry. 2007 Oct 2;46(39):11069-79. Epub 2007 Sep 1. PMID:17764159 doi:http://dx.doi.org/10.1021/bi7007245
|
