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| {{STRUCTURE_2gdr| PDB=2gdr | SCENE= }} | | {{STRUCTURE_2gdr| PDB=2gdr | SCENE= }} |
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| '''Crystal structure of a bacterial glutathione transferase'''
| | ===Crystal structure of a bacterial glutathione transferase=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16920719}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16920719 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16920719}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: N-term domain is mixed beta sheets and alpha helice]] | | [[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 Sun May 4 04:59:11 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:57:10 2008'' |
