2iv0
From Proteopedia
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| - | [[Image:2iv0.jpg|left|200px]] | + | [[Image:2iv0.jpg|left|200px]] |
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| - | '''THERMAL STABILITY OF ISOCITRATE DEHYDROGENASE FROM ARCHAEOGLOBUS FULGIDUS STUDIED BY CRYSTAL STRUCTURE ANALYSIS AND ENGINEERING OF CHIMERS''' | + | {{Structure |
| + | |PDB= 2iv0 |SIZE=350|CAPTION= <scene name='initialview01'>2iv0</scene>, resolution 2.50Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+B'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Isocitrate_dehydrogenase_(NADP(+)) Isocitrate dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.42 1.1.1.42] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THERMAL STABILITY OF ISOCITRATE DEHYDROGENASE FROM ARCHAEOGLOBUS FULGIDUS STUDIED BY CRYSTAL STRUCTURE ANALYSIS AND ENGINEERING OF CHIMERS''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2IV0 is a [ | + | 2IV0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IV0 OCA]. |
==Reference== | ==Reference== | ||
| - | Thermal stability of isocitrate dehydrogenase from Archaeoglobus fulgidus studied by crystal structure analysis and engineering of chimers., Stokke R, Karlstrom M, Yang N, Leiros I, Ladenstein R, Birkeland NK, Steen IH, Extremophiles. 2007 May;11(3):481-93. Epub 2007 Mar 31. PMID:[http:// | + | Thermal stability of isocitrate dehydrogenase from Archaeoglobus fulgidus studied by crystal structure analysis and engineering of chimers., Stokke R, Karlstrom M, Yang N, Leiros I, Ladenstein R, Birkeland NK, Steen IH, Extremophiles. 2007 May;11(3):481-93. Epub 2007 Mar 31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17401542 17401542] |
[[Category: Archaeoglobus fulgidus]] | [[Category: Archaeoglobus fulgidus]] | ||
[[Category: Isocitrate dehydrogenase (NADP(+))]] | [[Category: Isocitrate dehydrogenase (NADP(+))]] | ||
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[[Category: domain swapping]] | [[Category: domain swapping]] | ||
[[Category: glyoxylate bypass]] | [[Category: glyoxylate bypass]] | ||
| - | [[Category: ionic | + | [[Category: ionic network]] |
[[Category: isocitrate dehydrogenase]] | [[Category: isocitrate dehydrogenase]] | ||
[[Category: nadp]] | [[Category: nadp]] | ||
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[[Category: tricarboxylic acid cycle]] | [[Category: tricarboxylic acid cycle]] | ||
| - | ''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 17:33:42 2008'' |
Revision as of 15:33, 20 March 2008
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| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | and | ||||||
| Activity: | Isocitrate dehydrogenase (NADP(+)), with EC number 1.1.1.42 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THERMAL STABILITY OF ISOCITRATE DEHYDROGENASE FROM ARCHAEOGLOBUS FULGIDUS STUDIED BY CRYSTAL STRUCTURE ANALYSIS AND ENGINEERING OF CHIMERS
Overview
Isocitrate dehydrogenase from Archaeoglobus fulgidus (AfIDH) has an apparent melting temperature (T(m)) of 98.5 degrees C. To identify the structural features involved in thermal stabilization of AfIDH, the structure was solved to 2.5 A resolution. AfIDH was strikingly similar to mesophilic IDH from Escherichia coli (EcIDH) and displayed almost the same number of ion pairs and ionic networks. However, two unique inter-domain networks were present in AfIDH; one three-membered ionic network between the large and the small domain and one four-membered ionic network between the clasp and the small domain. The latter ionic network was presumably reduced in size when the clasp domain of AfIDH was swapped with that of EcIDH and the T (m) decreased by 18 degrees C. Contrarily, EcIDH was only stabilized by 4 degrees C by the clasp domain of AfIDH, a result probably due to the introduction of a unique inter-subunit aromatic cluster in AfIDH that may strengthen the dimeric interface in this enzyme. A unique aromatic cluster was identified close to the N-terminus of AfIDH that could provide additional stabilization of this region. Common and unique heat adaptive traits of AfIDH with those recently observed for hyperthermophilic IDH from Aeropyrum pernix (ApIDH) and Thermotoga maritima (TmIDH) are discussed herein.
About this Structure
2IV0 is a Single protein structure of sequence from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.
Reference
Thermal stability of isocitrate dehydrogenase from Archaeoglobus fulgidus studied by crystal structure analysis and engineering of chimers., Stokke R, Karlstrom M, Yang N, Leiros I, Ladenstein R, Birkeland NK, Steen IH, Extremophiles. 2007 May;11(3):481-93. Epub 2007 Mar 31. PMID:17401542
Page seeded by OCA on Thu Mar 20 17:33:42 2008
Categories: Archaeoglobus fulgidus | Isocitrate dehydrogenase (NADP(+)) | Single protein | Birkeland, N K. | Karlstrom, M. | Ladenstein, R. | Leiros, I. | Steen, I H. | Stokke, R. | Yang, N. | CL | ZN | Aromatic cluster | Domain swapping | Glyoxylate bypass | Ionic network | Isocitrate dehydrogenase | Nadp | Oxidoreductase | Phosphorylation | Thermal stability | Tricarboxylic acid cycle
