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| [[Image:1cr6.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1cr6| PDB=1cr6 | SCENE= }} | | {{STRUCTURE_1cr6| PDB=1cr6 | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF MURINE SOLUBLE EPOXIDE HYDROLASE COMPLEXED WITH CPU INHIBITOR'''
| | ===CRYSTAL STRUCTURE OF MURINE SOLUBLE EPOXIDE HYDROLASE COMPLEXED WITH CPU INHIBITOR=== |
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| ==Overview==
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| The crystal structure of recombinant murine liver cytosolic epoxide hydrolase (EC 3.3.2.3) has been determined at 2.8-A resolution. The binding of a nanomolar affinity inhibitor confirms the active site location in the C-terminal domain; this domain is similar to that of haloalkane dehalogenase and shares the alpha/beta hydrolase fold. A structure-based mechanism is proposed that illuminates the unique chemical strategy for the activation of endogenous and man-made epoxide substrates for hydrolysis and detoxification. Surprisingly, a vestigial active site is found in the N-terminal domain similar to that of another enzyme of halocarbon metabolism, haloacid dehalogenase. Although the vestigial active site does not participate in epoxide hydrolysis, the vestigial domain plays a critical structural role by stabilizing the dimer in a distinctive domain-swapped architecture. Given the genetic and structural relationships among these enzymes of xenobiotic metabolism, a structure-based evolutionary sequence is postulated. | | The line below this paragraph, {{ABSTRACT_PUBMED_10485878}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10485878 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10485878}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Disubstituted urea inhibitor]] | | [[Category: Disubstituted urea inhibitor]] |
| [[Category: Homodimer]] | | [[Category: Homodimer]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:02:00 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:11:48 2008'' |