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9icd
From Proteopedia
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[[Image:9icd.gif|left|200px]] | [[Image:9icd.gif|left|200px]] | ||
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'''CATALYTIC MECHANISM OF NADP+-DEPENDENT ISOCITRATE DEHYDROGENASE: IMPLICATIONS FROM THE STRUCTURES OF MAGNESIUM-ISOCITRATE AND NADP+ COMPLEXES''' | '''CATALYTIC MECHANISM OF NADP+-DEPENDENT ISOCITRATE DEHYDROGENASE: IMPLICATIONS FROM THE STRUCTURES OF MAGNESIUM-ISOCITRATE AND NADP+ COMPLEXES''' | ||
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Catalytic mechanism of NADP(+)-dependent isocitrate dehydrogenase: implications from the structures of magnesium-isocitrate and NADP+ complexes., Hurley JH, Dean AM, Koshland DE Jr, Stroud RM, Biochemistry. 1991 Sep 3;30(35):8671-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1888729 1888729] | Catalytic mechanism of NADP(+)-dependent isocitrate dehydrogenase: implications from the structures of magnesium-isocitrate and NADP+ complexes., Hurley JH, Dean AM, Koshland DE Jr, Stroud RM, Biochemistry. 1991 Sep 3;30(35):8671-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1888729 1888729] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: Isocitrate dehydrogenase (NADP(+))]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dean, A M.]] | [[Category: Dean, A M.]] | ||
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[[Category: Koshlandjunior, D E.]] | [[Category: Koshlandjunior, D E.]] | ||
[[Category: Stroud, R M.]] | [[Category: Stroud, R M.]] | ||
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Revision as of 19:53, 4 May 2008
CATALYTIC MECHANISM OF NADP+-DEPENDENT ISOCITRATE DEHYDROGENASE: IMPLICATIONS FROM THE STRUCTURES OF MAGNESIUM-ISOCITRATE AND NADP+ COMPLEXES
Overview
The structures of NADP+ and magnesium isocitrate bound to the NADP(+)-dependent isocitrate dehydrogenase of Escherichia coli have been determined and refined at 2.5-A resolution. NADP+ is bound by the large domain of isocitrate dehydrogenase, a structure that has little similarity to the supersecondary structure of the nucleotide-binding domain of the lactate dehydrogenase-like family of nucleotide-binding proteins. The coenzyme-binding site confirms the fundamentally different evolution of the isocitrate dehydrogenase-like and the lactate dehydrogenase-like classes of nucleotide-binding proteins. In the magnesium-isocitrate complex, magnesium is coordinated to the alpha-carboxylate and alpha-hydroxyl oxygen of isocitrate in a manner suitable for stabilization of a negative charge on the hydroxyl oxygen during both the dehydrogenation and decarboxylation steps of the conversion of isocitrate to alpha-ketoglutarate. The metal ion is also coordinated by aspartate side chains 283' (of the second subunit of the dimer) and 307 and two water molecules in a roughly octahedral arrangement. On the basis of the geometry of the active site, the base functioning in the dehydrogenation step is most likely aspartate 283'. E. coli isocitrate dehydrogenase transfers a hydride stereospecifically to the A-side of NADP+, and models for a reactive ternary complex consistent with this stereospecificity are discussed.
About this Structure
9ICD is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Catalytic mechanism of NADP(+)-dependent isocitrate dehydrogenase: implications from the structures of magnesium-isocitrate and NADP+ complexes., Hurley JH, Dean AM, Koshland DE Jr, Stroud RM, Biochemistry. 1991 Sep 3;30(35):8671-8. PMID:1888729 Page seeded by OCA on Sun May 4 22:53:16 2008
