2iv0: Difference between revisions
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[[Image:2iv0.jpg|left|200px]]<br /><applet load="2iv0" size=" | [[Image:2iv0.jpg|left|200px]]<br /><applet load="2iv0" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2iv0, resolution 2.50Å" /> | caption="2iv0, resolution 2.50Å" /> | ||
'''THERMAL STABILITY OF ISOCITRATE DEHYDROGENASE FROM ARCHAEOGLOBUS FULGIDUS STUDIED BY CRYSTAL STRUCTURE ANALYSIS AND ENGINEERING OF CHIMERS'''<br /> | '''THERMAL STABILITY OF ISOCITRATE DEHYDROGENASE FROM ARCHAEOGLOBUS FULGIDUS STUDIED BY CRYSTAL STRUCTURE ANALYSIS AND ENGINEERING OF CHIMERS'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2IV0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus] with ZN and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Site: <scene name='pdbsite=AC1:Cl Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http:// | 2IV0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Site: <scene name='pdbsite=AC1:Cl Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IV0 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: tricarboxylic acid cycle]] | [[Category: tricarboxylic acid cycle]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:37:51 2008'' | ||
Revision as of 15:37, 23 January 2008
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THERMAL STABILITY OF ISOCITRATE DEHYDROGENASE FROM ARCHAEOGLOBUS FULGIDUS STUDIED BY CRYSTAL STRUCTURE ANALYSIS AND ENGINEERING OF CHIMERS
OverviewOverview
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 StructureAbout this Structure
2IV0 is a Single protein structure of sequence from Archaeoglobus fulgidus with and as ligands. Active as Isocitrate dehydrogenase (NADP(+)), with EC number 1.1.1.42 Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
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
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- 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 networks
- Isocitrate dehydrogenase
- Nadp
- Oxidoreductase
- Phosphorylation
- Thermal stability
- Tricarboxylic acid cycle