2iv0: Difference between revisions

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Revision as of 03:49, 31 March 2008

File:2iv0.jpg

, resolution 2.50Å

Sites:

Ligands:

,

Activity:

Isocitrate dehydrogenase (NADP(+)), with EC number 1.1.1.42

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

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. 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

Page seeded by OCA on Mon Mar 31 03:49:02 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 4: / Line 4: @@
 |PDB= 2iv0 |SIZE=350|CAPTION= <scene name='initialview01'>2iv0</scene>, resolution 2.50&Aring;
 |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>
+|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]
+|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>
 |GENE=
+|DOMAIN=
+|RELATEDENTRY=
+|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>
 }}
@@ Line 30: / Line 33: @@
 [[Category: Stokke, R.]]
 [[Category: Yang, N.]]
-[[Category: CL]]
-[[Category: ZN]]
 [[Category: archaeoglobus fulgidus]]
 [[Category: aromatic cluster]]
@@ Line 44: / Line 45: @@
 [[Category: tricarboxylic acid cycle]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:33:42 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:49:02 2008''