2icj

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[[Image:2icj.jpg|left|200px]]
[[Image:2icj.jpg|left|200px]]
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{{Structure
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|PDB= 2icj |SIZE=350|CAPTION= <scene name='initialview01'>2icj</scene>, resolution 1.7&Aring;
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The line below this paragraph, containing "STRUCTURE_2icj", 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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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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|DOMAIN=
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{{STRUCTURE_2icj| PDB=2icj | SCENE= }}
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|RELATEDENTRY=[[2ick|2ICK]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2icj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2icj OCA], [http://www.ebi.ac.uk/pdbsum/2icj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2icj RCSB]</span>
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}}
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'''The crystal structure of human isopentenyl diphophate isomerase'''
'''The crystal structure of human isopentenyl diphophate isomerase'''
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[[Category: Rao, Z.]]
[[Category: Rao, Z.]]
[[Category: Zheng, W.]]
[[Category: Zheng, W.]]
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[[Category: crystal structure]]
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[[Category: Crystal structure]]
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[[Category: human isopentenyl diphophate isomerase]]
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[[Category: Human isopentenyl diphophate isomerase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:20:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:42:28 2008''
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Revision as of 04:20, 4 May 2008

Image:2icj.jpg

Template:STRUCTURE 2icj

The crystal structure of human isopentenyl diphophate isomerase


Overview

Isopentenyl diphosphate isomerase catalyses a crucial activation step in the biosynthesis of isoprenoids, one of the most ancient and diverse classes of natural products. This enzyme is responsible for an unusual isomerization of the inactive carbon-carbon double bond of isopentenyl diphosphate (IPP) to create its electrophilic allylic isomer dimethylallyl diphosphate (DMAPP). Here we report the crystal structure of human IPP isomerase at 1.7 A resolution and the complex structure with its native substrate at 1.9 A resolution. These structures reveal a mechanism wherein interconversion is catalyzed by a stereoselective antarafacial [1.3] transposition of a proton involving the indispensable residues Cys87, Glu149, Trp197 and Tyr137. A newly identified alternative conformation of Cys87 driven by Trp197 and the selectivity of different metal ions located in the active site provide further insight into the catalytic mechanism. Comparison with Escherichia coli IPP isomerase reveals a novel substrate entrance in human IPP isomerase.

About this Structure

2ICJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The crystal structure of human isopentenyl diphosphate isomerase at 1.7 A resolution reveals its catalytic mechanism in isoprenoid biosynthesis., Zheng W, Sun F, Bartlam M, Li X, Li R, Rao Z, J Mol Biol. 2007 Mar 9;366(5):1447-58. Epub 2006 Dec 24. PMID:17250851 Page seeded by OCA on Sun May 4 07:20:02 2008

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