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1nfs

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[[Image:1nfs.jpg|left|200px]]<br /><applet load="1nfs" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1nfs.jpg|left|200px]]
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caption="1nfs, resolution 1.96&Aring;" />
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'''STRUCTURE AND MECHANISM OF ACTION OF ISOPENTENYLPYROPHOSPHATE-DIMETHYLALLYLPYROPHOSPHATE ISOMERASE: COMPLEX WITH NIPP'''<br />
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{{Structure
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|PDB= 1nfs |SIZE=350|CAPTION= <scene name='initialview01'>1nfs</scene>, resolution 1.96&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=DED:2-DIMETHYLAMINO-ETHYL-DIPHOSPHATE'>DED</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''STRUCTURE AND MECHANISM OF ACTION OF ISOPENTENYLPYROPHOSPHATE-DIMETHYLALLYLPYROPHOSPHATE ISOMERASE: COMPLEX WITH NIPP'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1NFS 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=DED:'>DED</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=1NFS OCA].
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1NFS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NFS OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12540835 12540835]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12540835 12540835]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Isopentenyl-diphosphate Delta-isomerase]]
[[Category: Isopentenyl-diphosphate Delta-isomerase]]
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[[Category: complex]]
[[Category: complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:05:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:56:15 2008''

Revision as of 10:56, 20 March 2008

Image:1nfs.jpg


PDB ID 1nfs

Drag the structure with the mouse to rotate
, resolution 1.96Å
Ligands: , and
Activity: Isopentenyl-diphosphate Delta-isomerase, with EC number 5.3.3.2
Coordinates: save as pdb, mmCIF, xml



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


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

1NFS 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

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