2ick: Difference between revisions

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[[Image:2ick.jpg|left|200px]]
{{Seed}}
[[Image:2ick.png|left|200px]]


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{{STRUCTURE_2ick|  PDB=2ick  |  SCENE=  }}  
{{STRUCTURE_2ick|  PDB=2ick  |  SCENE=  }}  


'''Human isopentenyl diphophate isomerase complexed with substrate analog'''
===Human isopentenyl diphophate isomerase complexed with substrate analog===




==Overview==
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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.
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{{ABSTRACT_PUBMED_17250851}}


==About this Structure==
==About this Structure==
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[[Category: Human isopentenyl diphophate isomerase]]
[[Category: Human isopentenyl diphophate isomerase]]
[[Category: Substrate]]
[[Category: Substrate]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 07:20:04 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:50:54 2008''

Revision as of 14:50, 27 July 2008

File:2ick.png

Template:STRUCTURE 2ick

Human isopentenyl diphophate isomerase complexed with substrate analog

Template:ABSTRACT PUBMED 17250851

About this Structure

2ICK 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

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