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| {{STRUCTURE_2ibn| PDB=2ibn | SCENE= }} | | {{STRUCTURE_2ibn| PDB=2ibn | SCENE= }} |
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| '''Crystal structure of Human myo-Inositol Oxygenase (MIOX)'''
| | ===Crystal structure of Human myo-Inositol Oxygenase (MIOX)=== |
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| ==Overview==
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| Altered inositol metabolism is implicated in a number of diabetic complications. The first committed step in mammalian inositol catabolism is performed by myo-inositol oxygenase (MIOX), which catalyzes a unique four-electron dioxygen-dependent ring cleavage of myo-inositol to d-glucuronate. Here, we present the crystal structure of human MIOX in complex with myo-inosose-1 bound in a terminal mode to the MIOX diiron cluster site. Furthermore, from biochemical and biophysical results from N-terminal deletion mutagenesis we show that the N terminus is important, through coordination of a set of loops covering the active site, in shielding the active site during catalysis. EPR spectroscopy of the unliganded enzyme displays a two-component spectrum that we can relate to an open and a closed active site conformation. Furthermore, based on site-directed mutagenesis in combination with biochemical and biophysical data, we propose a novel role for Lys(127) in governing access to the diiron cluster.
| | The line below this paragraph, {{ABSTRACT_PUBMED_18364358}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 18364358 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_18364358}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Structural genomic]] | | [[Category: Structural genomic]] |
| [[Category: Structural genomics consortium]] | | [[Category: Structural genomics consortium]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 11 10:54:16 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:39:17 2008'' |