2dho

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[[Image:2dho.jpg|left|200px]]
[[Image:2dho.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 2dho |SIZE=350|CAPTION= <scene name='initialview01'>2dho</scene>, resolution 1.600&Aring;
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The line below this paragraph, containing "STRUCTURE_2dho", 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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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_2dho| PDB=2dho | SCENE= }}
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|RELATEDENTRY=[[2ewq|2EWQ]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dho OCA], [http://www.ebi.ac.uk/pdbsum/2dho PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2dho RCSB]</span>
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}}
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'''Crystal structure of human IPP isomerase I in space group P212121'''
'''Crystal structure of human IPP isomerase I in space group P212121'''
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[[Category: Wei, Z.]]
[[Category: Wei, Z.]]
[[Category: Zhang, C.]]
[[Category: Zhang, C.]]
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[[Category: alpha/beta protein]]
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[[Category: Alpha/beta protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 00:26:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:34:50 2008''
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Revision as of 21:26, 3 May 2008

Image:2dho.jpg

Template:STRUCTURE 2dho

Crystal structure of human IPP isomerase I in space group P212121


Overview

Type I isopentenyl diphosphate (IPP): dimethylally diphosphate (DMAPP) isomerase is an essential enzyme in human isoprenoid biosynthetic pathway. It catalyzes isomerization of the carbon-carbon double bonds in IPP and DMAPP, which are the basic building blocks for the subsequent biosynthesis. We have determined two crystal structures of human IPP isomerase I (hIPPI) under different crystallization conditions. High similarity between structures of human and Escherichia coli IPP isomerases proves the conserved catalytic mechanism. Unexpectedly, one of the hIPPI structures contains a natural substrate analog ethanol amine pyrophosphate (EAPP). Based on this structure, a water molecule is proposed to be the direct proton donor for IPP and different conformations of IPP and DMAPP bound in the enzyme are also proposed. In addition, structures of human IPPI show a flexible N-terminal alpha-helix covering the active pocket and blocking the entrance, which is absent in E. coli IPPI. Besides, the active site conformation is not the same in the two hIPPI structures. Such difference leads to a hypothesis that substrate binding induces conformational change in the active site. The inhibition mechanism of high Mn(2+) concentrations is also discussed.

About this Structure

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

Reference

Crystal structures of human IPP isomerase: new insights into the catalytic mechanism., Zhang C, Liu L, Xu H, Wei Z, Wang Y, Lin Y, Gong W, J Mol Biol. 2007 Mar 9;366(5):1437-46. Epub 2006 Nov 3. PMID:17137593 Page seeded by OCA on Sun May 4 00:26:53 2008

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