1nfz

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[[Image:1nfz.jpg|left|200px]]
[[Image:1nfz.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1nfz |SIZE=350|CAPTION= <scene name='initialview01'>1nfz</scene>, resolution 1.97&Aring;
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The line below this paragraph, containing "STRUCTURE_1nfz", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=EIP:4-HYDROXY-3-METHYL+BUTYL+DIPHOSPHATE'>EIP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1nfz| PDB=1nfz | SCENE= }}
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|RELATEDENTRY=[[1hzt|1HZT]], [[1hx3|1HX3]], [[1n2u|1N2U]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nfz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nfz OCA], [http://www.ebi.ac.uk/pdbsum/1nfz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nfz RCSB]</span>
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}}
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'''STRUCTURE AND MECHANISM OF ACTION OF ISOPENTENYLPYROPHOSPHATE-DIMETHYLALLYLPYROPHOSPHATE ISOMERASE: COMPLEX WITH EIPP'''
'''STRUCTURE AND MECHANISM OF ACTION OF ISOPENTENYLPYROPHOSPHATE-DIMETHYLALLYLPYROPHOSPHATE ISOMERASE: COMPLEX WITH EIPP'''
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Wouters, J.]]
[[Category: Wouters, J.]]
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[[Category: complex]]
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[[Category: Complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:29:08 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:29:49 2008''
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Revision as of 23:29, 2 May 2008

Image:1nfz.jpg

Template:STRUCTURE 1nfz

STRUCTURE AND MECHANISM OF ACTION OF ISOPENTENYLPYROPHOSPHATE-DIMETHYLALLYLPYROPHOSPHATE ISOMERASE: COMPLEX WITH EIPP


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.

About this Structure

1NFZ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Catalytic mechanism of Escherichia coli isopentenyl diphosphate isomerase involves Cys-67, Glu-116, and Tyr-104 as suggested by crystal structures of complexes with transition state analogues and irreversible inhibitors., Wouters J, Oudjama Y, Barkley SJ, Tricot C, Stalon V, Droogmans L, Poulter CD, J Biol Chem. 2003 Apr 4;278(14):11903-8. Epub 2003 Jan 22. PMID:12540835 Page seeded by OCA on Sat May 3 02:29:08 2008

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OCA

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