This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1ow2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(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...)
Line 1: Line 1:
-
[[Image:1ow2.jpg|left|200px]]<br /><applet load="1ow2" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[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==
-
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.
+
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==
-
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].
+
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==
Line 20: Line 20:
[[Category: complex]]
[[Category: complex]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:14:36 2007''
+
''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

Image:1ow2.jpg

1ow2, resolution 2.00Å

Drag the structure with the mouse to rotate

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

Page seeded by OCA on Thu Feb 21 14:22:15 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ow2"
Personal tools