1POY

SPERMIDINE/PUTRESCINE-BINDING PROTEIN COMPLEXED WITH SPERMIDINE (DIMER FORM)

1POY の概要

• エントリーDOI: 10.2210/pdb1poy/pdb
• 関連するPDBエントリー: 1POT
• 分子名称: SPERMIDINE/PUTRESCINE-BINDING PROTEIN, SPERMIDINE (3 entities in total)
• 機能のキーワード: transport protein, binding protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Periplasm: P23861
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 145772.50

構造登録者

Sugiyama, S.,Vassylyev, D.G.,Matsushima, M.,Morikawa, K. (登録日: 1996-02-02, 公開日: 1996-07-11, 最終更新日: 2024-02-14)

主引用文献

Sugiyama, S.,Vassylyev, D.G.,Matsushima, M.,Kashiwagi, K.,Igarashi, K.,Morikawa, K.
Crystal structure of PotD, the primary receptor of the polyamine transport system in Escherichia coli.
J.Biol.Chem., 271:9519-9525, 1996

PubMed Abstract: PotD protein is a periplasmic binding protein and the primary receptor of the polyamine transport system, which regulates the polyamine content in Escherichia coli. The crystal structure of PotD in complex with spermidine has been solved at 2.5-A resolution. The PotD protein consists of two domains with an alternating beta-alpha-beta topology. The polyamine binding site is in a central cleft lying in the interface between the domains. In the cleft, four acidic residues recognize the three positively charged nitrogen atoms of spermidine, while five aromatic side chains anchor the methylene backbone by van der Waals interactions. The overall fold of PotD is similar to that of other periplasmic binding proteins, and in particular to the maltodextrin-binding protein from E. coli, despite the fact that sequence identity is as low as 20%. The comparison of the PotD structure with the two maltodextrin-binding protein structures, determined in the presence and absence of the substrate, suggests that spermidine binding rearranges the relative orientation of the PotD domains to create a more compact structure.

PubMed: 8621624
DOI: 10.1074/jbc.271.16.9519

実験手法

X-RAY DIFFRACTION (2.5 Å)