2iv0

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[[Image:2iv0.jpg|left|200px]]
[[Image:2iv0.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 2iv0 |SIZE=350|CAPTION= <scene name='initialview01'>2iv0</scene>, resolution 2.50&Aring;
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The line below this paragraph, containing "STRUCTURE_2iv0", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+B'>AC1</scene>
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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=ZN:ZINC+ION'>ZN</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/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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_2iv0| PDB=2iv0 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2iv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iv0 OCA], [http://www.ebi.ac.uk/pdbsum/2iv0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2iv0 RCSB]</span>
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}}
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'''THERMAL STABILITY OF ISOCITRATE DEHYDROGENASE FROM ARCHAEOGLOBUS FULGIDUS STUDIED BY CRYSTAL STRUCTURE ANALYSIS AND ENGINEERING OF CHIMERS'''
'''THERMAL STABILITY OF ISOCITRATE DEHYDROGENASE FROM ARCHAEOGLOBUS FULGIDUS STUDIED BY CRYSTAL STRUCTURE ANALYSIS AND ENGINEERING OF CHIMERS'''
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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]
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]]
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[[Category: Isocitrate dehydrogenase (NADP(+))]]
 
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Birkeland, N K.]]
[[Category: Birkeland, N K.]]
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[[Category: Stokke, R.]]
[[Category: Stokke, R.]]
[[Category: Yang, N.]]
[[Category: Yang, N.]]
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[[Category: archaeoglobus fulgidus]]
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[[Category: Archaeoglobus fulgidus]]
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[[Category: aromatic cluster]]
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[[Category: Aromatic cluster]]
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[[Category: domain swapping]]
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[[Category: Domain swapping]]
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[[Category: glyoxylate bypass]]
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[[Category: Glyoxylate bypass]]
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[[Category: ionic network]]
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[[Category: Ionic network]]
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[[Category: isocitrate dehydrogenase]]
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[[Category: Isocitrate dehydrogenase]]
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[[Category: nadp]]
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[[Category: Nadp]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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[[Category: phosphorylation]]
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[[Category: Phosphorylation]]
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[[Category: thermal stability]]
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[[Category: Thermal stability]]
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[[Category: tricarboxylic acid cycle]]
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[[Category: Tricarboxylic acid cycle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:55:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:49:02 2008''
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Revision as of 04:55, 4 May 2008

Image:2iv0.jpg

Template:STRUCTURE 2iv0

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 Sun May 4 07:55:18 2008

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