1nfz: Difference between revisions

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New page: left|200px<br /><applet load="1nfz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nfz, resolution 1.97Å" /> '''STRUCTURE AND MECHAN...
 
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[[Image:1nfz.jpg|left|200px]]<br /><applet load="1nfz" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1nfz.jpg|left|200px]]<br /><applet load="1nfz" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1nfz, resolution 1.97&Aring;" />
caption="1nfz, resolution 1.97&Aring;" />
'''STRUCTURE AND MECHANISM OF ACTION OF ISOPENTENYLPYROPHOSPHATE-DIMETHYLALLYLPYROPHOSPHATE ISOMERASE: COMPLEX WITH EIPP'''<br />
'''STRUCTURE AND MECHANISM OF ACTION OF ISOPENTENYLPYROPHOSPHATE-DIMETHYLALLYLPYROPHOSPHATE ISOMERASE: COMPLEX WITH EIPP'''<br />


==Overview==
==Overview==
Isopentenyl diphosphate (IPP):dimethylallyl diphosphate (DMAPP) isomerase, is a key enzyme in the biosynthesis of isoprenoids. The reaction involves, protonation and deprotonation of the isoprenoid unit and proceeds through, a carbocationic transition state. Analysis of the crystal structures (2 A), of complexes of Escherichia coli IPP.DMAPPs isomerase with a transition, state analogue (N,N-dimethyl-2-amino-1-ethyl diphosphate) and a covalently, attached irreversible inhibitor (3,4-epoxy-3-methyl-1-butyl diphosphate), indicates that Glu-116, Tyr-104, and Cys-67 are involved in the, antarafacial addition/elimination of protons during isomerization. This, work provides a new perspective about the mechanism of the reaction.
Isopentenyl diphosphate (IPP):dimethylallyl diphosphate (DMAPP) isomerase is a key enzyme in the biosynthesis of isoprenoids. The reaction involves protonation and deprotonation of the isoprenoid unit and proceeds through a carbocationic transition state. Analysis of the crystal structures (2 A) of complexes of Escherichia coli IPP.DMAPPs isomerase with a transition state analogue (N,N-dimethyl-2-amino-1-ethyl diphosphate) and a covalently attached irreversible inhibitor (3,4-epoxy-3-methyl-1-butyl diphosphate) indicates that Glu-116, Tyr-104, and Cys-67 are involved in the antarafacial addition/elimination of protons during isomerization. This work provides a new perspective about the mechanism of the reaction.


==About this Structure==
==About this Structure==
1NFZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MN, MG and EIP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Isopentenyl-diphosphate_Delta-isomerase Isopentenyl-diphosphate Delta-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.3.2 5.3.3.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NFZ OCA].  
1NFZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=EIP:'>EIP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Isopentenyl-diphosphate_Delta-isomerase Isopentenyl-diphosphate Delta-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.3.2 5.3.3.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NFZ OCA].  


==Reference==
==Reference==
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[[Category: complex]]
[[Category: complex]]


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