1ow2

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(New page: 200px<br /><applet load="1ow2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ow2, resolution 2.00&Aring;" /> '''STRUCTURE AND MECHAN...)
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[[Image:1ow2.jpg|left|200px]]<br /><applet load="1ow2" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ow2, resolution 2.00&Aring;" />
caption="1ow2, resolution 2.00&Aring;" />
'''STRUCTURE AND MECHANISM OF ACTION OF ISOPENTENYLPYROPHOSPHATE-DIMETHYLALLYLPYROPHOSPHATE ISOMERASE: COMPLEX OF C67A MUTANT WITH EIPP'''<br />
'''STRUCTURE AND MECHANISM OF ACTION OF ISOPENTENYLPYROPHOSPHATE-DIMETHYLALLYLPYROPHOSPHATE ISOMERASE: COMPLEX OF C67A MUTANT WITH EIPP'''<br />
==Overview==
==Overview==
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Isopentenyl diphosphate:dimethylallyl diphosphate (IPP:DMAPP) isomerase is, a key enzyme in the biosynthesis of isoprenoids. The mechanism of the, isomerization reaction involves protonation of the unactivated, carbon-carbon double bond in the substrate. Analysis of the 1.97 A crystal, structure of the inactive C67A mutant of E. coli isopentenyl, diphosphate:dimethylallyl diphosphate isomerase complexed with the, mechanism-based inactivator 3,4-epoxy-3-methyl-1-butyl diphosphate is in, agreement with an isomerization mechanism involving Glu 116, Tyr 104, and, Cys 67. In particular, the results are consistent with a mechanism where, Glu116 is involved in the protonation step and Cys67 in the elimination, step.
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Isopentenyl diphosphate:dimethylallyl diphosphate (IPP:DMAPP) isomerase is a key enzyme in the biosynthesis of isoprenoids. The mechanism of the isomerization reaction involves protonation of the unactivated carbon-carbon double bond in the substrate. Analysis of the 1.97 A crystal structure of the inactive C67A mutant of E. coli isopentenyl diphosphate:dimethylallyl diphosphate isomerase complexed with the mechanism-based inactivator 3,4-epoxy-3-methyl-1-butyl diphosphate is in agreement with an isomerization mechanism involving Glu 116, Tyr 104, and Cys 67. In particular, the results are consistent with a mechanism where Glu116 is involved in the protonation step and Cys67 in the elimination step.
==About this Structure==
==About this Structure==
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1OW2 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=1OW2 OCA].
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1OW2 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=1OW2 OCA].
==Reference==
==Reference==
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[[Category: complex]]
[[Category: complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:14:36 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:22:15 2008''

Revision as of 12:22, 21 February 2008


1ow2, resolution 2.00Å

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STRUCTURE AND MECHANISM OF ACTION OF ISOPENTENYLPYROPHOSPHATE-DIMETHYLALLYLPYROPHOSPHATE ISOMERASE: COMPLEX OF C67A MUTANT WITH EIPP

Overview

Isopentenyl diphosphate:dimethylallyl diphosphate (IPP:DMAPP) isomerase is a key enzyme in the biosynthesis of isoprenoids. The mechanism of the isomerization reaction involves protonation of the unactivated carbon-carbon double bond in the substrate. Analysis of the 1.97 A crystal structure of the inactive C67A mutant of E. coli isopentenyl diphosphate:dimethylallyl diphosphate isomerase complexed with the mechanism-based inactivator 3,4-epoxy-3-methyl-1-butyl diphosphate is in agreement with an isomerization mechanism involving Glu 116, Tyr 104, and Cys 67. In particular, the results are consistent with a mechanism where Glu116 is involved in the protonation step and Cys67 in the elimination step.

About this Structure

1OW2 is a Single protein structure of sequence from Escherichia coli with , and as ligands. Active as Isopentenyl-diphosphate Delta-isomerase, with EC number 5.3.3.2 Full crystallographic information is available from OCA.

Reference

Crystal structure of the C67A mutant of isopentenyl diphosphate isomerase complexed with a mechanism-based irreversible inhibitor., Wouters J, Oudjama Y, Stalon V, Droogmans L, Poulter CD, Proteins. 2004 Feb 1;54(2):216-21. PMID:14696183

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