1hx3
From Proteopedia
(New page: 200px<br /><applet load="1hx3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hx3, resolution 2.1Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1hx3.gif|left|200px]]<br /><applet load="1hx3" size=" | + | [[Image:1hx3.gif|left|200px]]<br /><applet load="1hx3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hx3, resolution 2.1Å" /> | caption="1hx3, resolution 2.1Å" /> | ||
'''CRYSTAL STRUCTURE OF E.COLI ISOPENTENYL DIPHOSPHATE:DIMETHYLALLYL DIPHOSPHATE ISOMERASE'''<br /> | '''CRYSTAL STRUCTURE OF E.COLI ISOPENTENYL DIPHOSPHATE:DIMETHYLALLYL DIPHOSPHATE ISOMERASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Isopentenyl diphosphate:dimethylallyl diphosphate (IPP:DMAPP) isomerase | + | Isopentenyl diphosphate:dimethylallyl diphosphate (IPP:DMAPP) isomerase catalyses a crucial activation step in the isoprenoid biosynthesis pathway. This enzyme is responsible for the isomerization of the carbon-carbon double bond of IPP to create the potent electrophile DMAPP. DMAPP then alkylates other molecules, including IPP, to initiate the extraordinary variety of isoprenoid compounds found in nature. The crystal structures of free and metal-bound Escherichia coli IPP isomerase reveal critical active site features underlying its catalytic mechanism. The enzyme requires one Mn(2+) or Mg(2+) ion to fold in its active conformation, forming a distorted octahedral metal coordination site composed of three histidines and two glutamates and located in the active site. Two critical residues, C67 and E116, face each other within the active site, close to the metal-binding site. The structures are compatible with a mechanism in which the cysteine initiates the reaction by protonating the carbon-carbon double bond, with the antarafacial rearrangement ultimately achieved by one of the glutamates involved in the metal coordination sphere. W161 may stabilize the highly reactive carbocation generated during the reaction through quadrupole- charge interaction. |
==About this Structure== | ==About this Structure== | ||
| - | 1HX3 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 SO4, MN and IMD 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:// | + | 1HX3 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=SO4:'>SO4</scene>, <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=IMD:'>IMD</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=1HX3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: isoprenoids]] | [[Category: isoprenoids]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:05:41 2008'' |
Revision as of 11:05, 21 February 2008
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CRYSTAL STRUCTURE OF E.COLI ISOPENTENYL DIPHOSPHATE:DIMETHYLALLYL DIPHOSPHATE ISOMERASE
Overview
Isopentenyl diphosphate:dimethylallyl diphosphate (IPP:DMAPP) isomerase catalyses a crucial activation step in the isoprenoid biosynthesis pathway. This enzyme is responsible for the isomerization of the carbon-carbon double bond of IPP to create the potent electrophile DMAPP. DMAPP then alkylates other molecules, including IPP, to initiate the extraordinary variety of isoprenoid compounds found in nature. The crystal structures of free and metal-bound Escherichia coli IPP isomerase reveal critical active site features underlying its catalytic mechanism. The enzyme requires one Mn(2+) or Mg(2+) ion to fold in its active conformation, forming a distorted octahedral metal coordination site composed of three histidines and two glutamates and located in the active site. Two critical residues, C67 and E116, face each other within the active site, close to the metal-binding site. The structures are compatible with a mechanism in which the cysteine initiates the reaction by protonating the carbon-carbon double bond, with the antarafacial rearrangement ultimately achieved by one of the glutamates involved in the metal coordination sphere. W161 may stabilize the highly reactive carbocation generated during the reaction through quadrupole- charge interaction.
About this Structure
1HX3 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 isopentenyl diphosphate:dimethylallyl diphosphate isomerase., Durbecq V, Sainz G, Oudjama Y, Clantin B, Bompard-Gilles C, Tricot C, Caillet J, Stalon V, Droogmans L, Villeret V, EMBO J. 2001 Apr 2;20(7):1530-7. PMID:11285217
Page seeded by OCA on Thu Feb 21 13:05:41 2008
Categories: Escherichia coli | Isopentenyl-diphosphate Delta-isomerase | Single protein | Bompard-Gilles, C. | Caillet, J. | Clantin, B. | Droogmans, L. | Durbecq, V. | Oudjama, Y. | Sainz, G. | Stalon, V. | Tricot, C. | Villeret, V. | IMD | MN | SO4 | Dimethylallyl | Isomerase | Isopentenyl | Isoprenoids
