1DL3

CRYSTAL STRUCTURE OF MUTUALLY GENERATED MONOMERS OF DIMERIC PHOSPHORIBOSYLANTRANILATE ISOMERASE FROM THERMOTOGA MARITIMA

1DL3 の概要

• エントリーDOI: 10.2210/pdb1dl3/pdb
• 関連するPDBエントリー: 1NSJ
• 分子名称: PROTEIN (PHOSPHORIBOSYLANTRANILATE ISOMERASE), SULFATE ION (3 entities in total)
• 機能のキーワード: isomerase, oligomerisation, thermostability, thermotoga maritima, protein engineering, dimer evolution
• 由来する生物種: Thermotoga maritima
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 46138.82

構造登録者

Thoma, R.,Hennig, M.,Sterner, R.,Kirschner, K. (登録日: 1999-12-08, 公開日: 1999-12-27, 最終更新日: 2024-02-07)

主引用文献

Thoma, R.,Hennig, M.,Sterner, R.,Kirschner, K.
Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima.
Structure Fold.Des., 8:265-276, 2000

PubMed Abstract: Oligomeric proteins may have been selected for in hyperthermophiles because subunit association provides extra stabilization. Phosphoribosylanthranilate isomerase (PRAI) is monomeric and labile in most mesophilic microorganisms, but dimeric and stable in the hyperthermophile Thermotoga maritima (tPRAI). The two subunits of tPRAI are associated back-to-back and are locked together by a hydrophobic loop. The hypothesis that dimerization is important for thermostability has been tested by rationally designing monomeric variants of tPRAI.

PubMed: 10745009
DOI: 10.1016/S0969-2126(00)00106-4

実験手法

X-RAY DIFFRACTION (2.7 Å)