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

1H98

New Insights into Thermostability of Bacterial Ferredoxins: High Resolution Crystal Structure of the Seven-Iron Ferredoxin from Thermus thermophilus

1H98 の概要
エントリーDOI10.2210/pdb1h98/pdb
分子名称FERREDOXIN, IRON/SULFUR CLUSTER, FE3-S4 CLUSTER, ... (4 entities in total)
機能のキーワードelectron transport, thermophilic, iron-sulfur, azotobacter, hydrogen bonds, stability, high resolution
由来する生物種THERMUS AQUATICUS
タンパク質・核酸の鎖数1
化学式量合計9341.30
構造登録者
Macedo-Ribeiro, S.,Martins, B.M.,Pereira, P.J.B.,Buse, G.,Huber, R.,Soulimane, T. (登録日: 2001-03-05, 公開日: 2001-11-27, 最終更新日: 2023-12-13)
主引用文献Macedo-Ribeiro, S.,Martins, B.M.,Pereira, P.J.B.,Buse, G.,Huber, R.,Soulimane, T.
New Insights Into the Thermostability of Bacterial Ferredoxins: High-Resolution Crystal Structure of the Seven-Iron Ferredoxin from Thermus Thermophilus
J.Biol.Inorg.Chem., 6:663-, 2001
Cited by
PubMed Abstract: The crystal structure of the seven-iron ferredoxin from Thermus thermophilus (FdTt) has been determined at 1.64 A resolution, allowing us to unveil the common mechanisms of thermostabilization within "bacterial-type" ferredoxins. FdTt and other homologous thermophilic seven-iron ferredoxins are smaller than their mesophilic counterparts. Thermostabilizing features are optimized in a minimal structural and functional unit, with an extensive cross-linking of secondary structure elements mediated by improved polar and hydrophobic interactions. Most of the potentially stabilizing features are focused on the vicinity of the functional [3Fe-4S] cluster. The structural [4Fe-4S] cluster is shielded in thermophilic FdTt by an increased number of polar interactions involving the two N-terminal residues. Comparisons with the hyperthermostable ferredoxin from Thermotoga maritima reveal that (1) a reduction in the number of non-glycine residues in strained conformations, (2) improved polar interactions within the common iron-sulfur cluster binding (betaalphabeta)2 motif, and (3) an optimized charge distribution at the protein surface, constitute a common strategy for increasing the thermal stability of these ferredoxins.
PubMed: 11681700
DOI: 10.1007/S007750100243
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.64 Å)
構造検証レポート
Validation report summary of 1h98
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