2cjp
From Proteopedia
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| - | [[Image:2cjp.gif|left|200px]]<br /> | + | [[Image:2cjp.gif|left|200px]]<br /><applet load="2cjp" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2cjp" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="2cjp, resolution 1.95Å" /> | caption="2cjp, resolution 1.95Å" /> | ||
'''STRUCTURE OF POTATO (SOLANUM TUBEROSUM) EPOXIDE HYDROLASE I (STEH1)'''<br /> | '''STRUCTURE OF POTATO (SOLANUM TUBEROSUM) EPOXIDE HYDROLASE I (STEH1)'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2CJP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Solanum_tuberosum Solanum tuberosum] with PG4, VPR and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_3.3.2.9 Transferred entry: 3.3.2.9], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.3 3.3.2.3] | + | 2CJP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Solanum_tuberosum Solanum tuberosum] with PG4, VPR and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_3.3.2.9 Transferred entry: 3.3.2.9], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.3 3.3.2.3] Known structural/functional Site: <scene name='pdbsite=AC1:Edo Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CJP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 19:25:37 2007'' |
Revision as of 17:15, 18 December 2007
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STRUCTURE OF POTATO (SOLANUM TUBEROSUM) EPOXIDE HYDROLASE I (STEH1)
Overview
Epoxide hydrolases catalyze the conversion of epoxides to diols. The known, functions of such enzymes include detoxification of xenobiotics, drug, metabolism, synthesis of signaling compounds, and intermediary metabolism., In plants, epoxide hydrolases are thought to participate in general, defense systems. In the present study, we report the first structure of a, plant epoxide hydrolase, one of the four homologous enzymes found in, potato. The structure was solved by molecular replacement and refined to a, resolution of 1.95 A. Analysis of the structure allows a better, understanding of the observed substrate specificities and activity., Further, comparisons with mammalian and fungal epoxide hydrolase, structures reported earlier show the basis of differing substrate, specificities in the various epoxide hydrolase subfamilies. Most plant, enzymes, like the potato epoxide hydrolase, are expected to be monomers, with a preference for substrates with long lipid-like substituents of the, epoxide ring. The significance of these results in the context of, biological roles and industrial applications is discussed.
About this Structure
2CJP is a Single protein structure of sequence from Solanum tuberosum with PG4, VPR and EDO as ligands. Active as Transferred entry: 3.3.2.9, with EC number 3.3.2.3 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
X-ray structure of potato epoxide hydrolase sheds light on substrate specificity in plant enzymes., Mowbray SL, Elfstrom LT, Ahlgren KM, Andersson CE, Widersten M, Protein Sci. 2006 Jul;15(7):1628-37. Epub 2006 Jun 2. PMID:16751602
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