2dho: Difference between revisions
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[[Image:2dho.jpg|left|200px]] | [[Image:2dho.jpg|left|200px]] | ||
'''Crystal structure of human IPP isomerase I in space group P212121''' | {{Structure | ||
|PDB= 2dho |SIZE=350|CAPTION= <scene name='initialview01'>2dho</scene>, resolution 1.600Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''Crystal structure of human IPP isomerase I in space group P212121''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2DHO is a [ | 2DHO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DHO OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17137593 17137593] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Isopentenyl-diphosphate Delta-isomerase]] | [[Category: Isopentenyl-diphosphate Delta-isomerase]] | ||
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[[Category: alpha/beta protein]] | [[Category: alpha/beta protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:27:19 2008'' | ||
Revision as of 17:27, 20 March 2008
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| , resolution 1.600Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Activity: | Isopentenyl-diphosphate Delta-isomerase, with EC number 5.3.3.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of human IPP isomerase I in space group P212121
OverviewOverview
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 StructureAbout this Structure
2DHO is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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
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