Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2IV0

Thermal stability of isocitrate dehydrogenase from Archaeoglobus fulgidus studied by crystal structure analysis and engineering of chimers

2IV0 の概要
エントリーDOI10.2210/pdb2iv0/pdb
分子名称ISOCITRATE DEHYDROGENASE, ZINC ION, CHLORIDE ION, ... (4 entities in total)
機能のキーワードoxidoreductase, archaeoglobus fulgidus, tricarboxylic acid cycle, isocitrate dehydrogenase, domain swapping, phosphorylation, aromatic cluster, nadp, ionic networks, thermal stability, glyoxylate bypass
由来する生物種ARCHAEOGLOBUS FULGIDUS
タンパク質・核酸の鎖数2
化学式量合計92489.44
構造登録者
Stokke, R.,Karlstrom, M.,Yang, N.,Leiros, I.,Ladenstein, R.,Birkeland, N.K.,Steen, I.H. (登録日: 2006-06-08, 公開日: 2007-04-17, 最終更新日: 2023-12-13)
主引用文献Stokke, R.,Karlstrom, M.,Yang, N.,Leiros, I.,Ladenstein, R.,Birkeland, N.K.,Steen, I.H.
Thermal Stability of Isocitrate Dehydrogenase from Archaeoglobus Fulgidus Studied by Crystal Structure Analysis and Engineering of Chimers
Extremophiles, 11:481-, 2007
Cited by
PubMed Abstract: 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.
PubMed: 17401542
DOI: 10.1007/S00792-006-0060-Z
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.5 Å)
構造検証レポート
Validation report summary of 2iv0
検証レポート(詳細版)ダウンロードをダウンロード

252091

件を2026-04-15に公開中

PDB statisticsPDBj update infoContact PDBjnumon