2gdr
From Proteopedia
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| - | [[Image:2gdr.gif|left|200px]] | + | [[Image:2gdr.gif|left|200px]] |
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| - | '''Crystal structure of a bacterial glutathione transferase''' | + | {{Structure |
| + | |PDB= 2gdr |SIZE=350|CAPTION= <scene name='initialview01'>2gdr</scene>, resolution 2.1Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=GTT:GLUTATHIONE'>GTT</scene> | ||
| + | |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] | ||
| + | |GENE= bphK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=36873 Burkholderia xenovorans]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of a bacterial glutathione transferase''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2GDR is a [ | + | 2GDR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Burkholderia_xenovorans Burkholderia xenovorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GDR OCA]. |
==Reference== | ==Reference== | ||
| - | Structures of ternary complexes of BphK, a bacterial glutathione S-transferase that reductively dechlorinates polychlorinated biphenyl metabolites., Tocheva EI, Fortin PD, Eltis LD, Murphy ME, J Biol Chem. 2006 Oct 13;281(41):30933-40. Epub 2006 Aug 17. PMID:[http:// | + | Structures of ternary complexes of BphK, a bacterial glutathione S-transferase that reductively dechlorinates polychlorinated biphenyl metabolites., Tocheva EI, Fortin PD, Eltis LD, Murphy ME, J Biol Chem. 2006 Oct 13;281(41):30933-40. Epub 2006 Aug 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16920719 16920719] |
[[Category: Burkholderia xenovorans]] | [[Category: Burkholderia xenovorans]] | ||
[[Category: Glutathione transferase]] | [[Category: Glutathione transferase]] | ||
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[[Category: GTT]] | [[Category: GTT]] | ||
[[Category: c-term domain is alpha helical]] | [[Category: c-term domain is alpha helical]] | ||
| - | [[Category: each monomer contains two | + | [[Category: each monomer contains two domain]] |
| - | [[Category: n-term domain is mixed beta sheets and alpha | + | [[Category: n-term domain is mixed beta sheets and alpha helice]] |
[[Category: protein homodimer]] | [[Category: protein homodimer]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:03:28 2008'' |
Revision as of 15:03, 20 March 2008
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| , resolution 2.1Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | bphK (Burkholderia xenovorans) | ||||||
| Activity: | Glutathione transferase, with EC number 2.5.1.18 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of a bacterial glutathione transferase
Overview
Prokaryotic glutathione S-transferases are as diverse as their eukaryotic counterparts but are much less well characterized. BphK from Burkholderia xenovorans LB400 consumes two GSH molecules to reductively dehalogenate chlorinated 2-hydroxy-6-oxo-6-phenyl-2,4-dienoates (HOPDAs), inhibitory polychlorinated biphenyl metabolites. Crystallographic structures of two ternary complexes of BphK were solved to a resolution of 2.1A. In the BphK-GSH-HOPDA complex, GSH and HOPDA molecules occupy the G- and H-subsites, respectively. The thiol nucleophile of the GSH molecule is positioned for SN2 attack at carbon 3 of the bound HOPDA. The respective sulfur atoms of conserved Cys-10 and the bound GSH are within 3.0A, consistent with product release and the formation of a mixed disulfide intermediate. In the BphK-(GSH)2 complex, a GSH molecule occupies each of the two subsites. The three sulfur atoms of the two GSH molecules and Cys-10 are aligned suitably for a disulfide exchange reaction that would regenerate the resting enzyme and yield disulfide-linked GSH molecules. A second conserved residue, His-106, is adjacent to the thiols of Cys-10 and the GSH bound to the G-subsite and thus may stabilize a transition state in the disulfide exchange reaction. Overall, the structures support and elaborate a proposed dehalogenation mechanism for BphK and provide insight into the plasticity of the H-subsite.
About this Structure
2GDR is a Single protein structure of sequence from Burkholderia xenovorans. Full crystallographic information is available from OCA.
Reference
Structures of ternary complexes of BphK, a bacterial glutathione S-transferase that reductively dechlorinates polychlorinated biphenyl metabolites., Tocheva EI, Fortin PD, Eltis LD, Murphy ME, J Biol Chem. 2006 Oct 13;281(41):30933-40. Epub 2006 Aug 17. PMID:16920719
Page seeded by OCA on Thu Mar 20 17:03:28 2008
