4ofw: Difference between revisions
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<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=4ofw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ofw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ofw RCSB], [http://www.ebi.ac.uk/pdbsum/4ofw 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=4ofw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ofw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ofw RCSB], [http://www.ebi.ac.uk/pdbsum/4ofw PDBsum]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
DJ-1 family proteins have recently been characterized as novel glyoxalases, although their cofactor-free catalytic mechanisms are not fully understood. In this work, we obtained crystals of Arabidopsis thaliana DJ-1d (atDJ-1d) and Homo sapiens DJ-1 (hDJ-1) covalently bound to glyoxylate, an analog of methylglyoxal, forming a hemithioacetal that presumably mimics an intermediate structure in the catalysis from methylglyoxal to lactate. The level of deuteration in lactate formation supported the proton transfer mechanism in the enzyme reaction. Differences in the enantiomeric specificity of D/L-lactacte formation observed in the DJ-1 superfamily proteins were explained by the presence of a His residue in the active site with essential Cys and Glu residues. The model for the stereospecificity was further evaluated by a molecular modeling simulation with methylglyoxal hemithioacetal superimposed on the glyoxylate hemithioacetal. The DJ-1 glyoxalase provides a unique mechanism in understanding the His residue-involved stereospecificity. This article is protected by copyright. All rights reserved. | |||
Stereospecific mechanism of DJ-1 glyoxalases inferred from their hemithioacetal-containing crystal structures.,Choi D, Kim J, Ha S, Kwon K, Kim EH, Lee HY, Ryu KS, Park C FEBS J. 2014 Oct 4. doi: 10.1111/febs.13085. PMID:25283443<ref>PMID:25283443</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | |||
<references/> | |||
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</StructureSection> | </StructureSection> | ||
Revision as of 11:14, 22 October 2014
Crystal Structure of Arabidopsis thaliana DJ-1dCrystal Structure of Arabidopsis thaliana DJ-1d
Structural highlights
Publication Abstract from PubMedDJ-1 family proteins have recently been characterized as novel glyoxalases, although their cofactor-free catalytic mechanisms are not fully understood. In this work, we obtained crystals of Arabidopsis thaliana DJ-1d (atDJ-1d) and Homo sapiens DJ-1 (hDJ-1) covalently bound to glyoxylate, an analog of methylglyoxal, forming a hemithioacetal that presumably mimics an intermediate structure in the catalysis from methylglyoxal to lactate. The level of deuteration in lactate formation supported the proton transfer mechanism in the enzyme reaction. Differences in the enantiomeric specificity of D/L-lactacte formation observed in the DJ-1 superfamily proteins were explained by the presence of a His residue in the active site with essential Cys and Glu residues. The model for the stereospecificity was further evaluated by a molecular modeling simulation with methylglyoxal hemithioacetal superimposed on the glyoxylate hemithioacetal. The DJ-1 glyoxalase provides a unique mechanism in understanding the His residue-involved stereospecificity. This article is protected by copyright. All rights reserved. Stereospecific mechanism of DJ-1 glyoxalases inferred from their hemithioacetal-containing crystal structures.,Choi D, Kim J, Ha S, Kwon K, Kim EH, Lee HY, Ryu KS, Park C FEBS J. 2014 Oct 4. doi: 10.1111/febs.13085. PMID:25283443[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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