4Q8R

Crystal structure of a Phosphate Binding Protein (PBP-1) from Clostridium perfringens

4Q8R の概要

• エントリーDOI: 10.2210/pdb4q8r/pdb
• 関連するPDBエントリー: 4GD5
• 分子名称: Phosphate ABC transporter, phosphate-binding protein, PHOSPHATE ION, ZINC ION, ... (4 entities in total)
• 機能のキーワード: periplasmic high affinity phosphate binding protein, transport protein
• 由来する生物種: Clostridium perfringens
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27635.08

構造登録者

Gonzalez, D.,Richez, M.,Bergonzi, C.,Chabriere, E.,Elias, M. (登録日: 2014-04-28, 公開日: 2014-11-05, 最終更新日: 2023-09-20)

主引用文献

Gonzalez, D.,Richez, M.,Bergonzi, C.,Chabriere, E.,Elias, M.
Crystal structure of the phosphate-binding protein (PBP-1) of an ABC-type phosphate transporter from Clostridium perfringens.
Sci Rep, 4:6636-6636, 2014

PubMed Abstract: Phosphate limitation is an important environmental stress that affects the metabolism of various organisms and, in particular, can trigger the virulence of numerous bacterial pathogens. Clostridium perfringens, a human pathogen, is one of the most common causes of enteritis necroticans, gas gangrene and food poisoning. Here, we focused on the high affinity phosphate-binding protein (PBP-1) of an ABC-type transporter, responsible for cellular phosphate uptake. We report the crystal structure (1.65 Å resolution) of the protein in complex with phosphate. Interestingly, PBP-1 does not form the short, low-barrier hydrogen bond with phosphate that is typical of previously characterized phosphate-binding proteins, but rather a canonical hydrogen bond. In its unique binding configuration, PBP-1 forms an unusually high number of hydrogen bonds (14) with the phosphate anion. Discrimination experiments reveal that PBP-1 is the least selective PBP characterised so far and is able to discriminate phosphate from its close competing anion, arsenate, by ~150-fold.

PubMed: 25338617
DOI: 10.1038/srep06636

実験手法

X-RAY DIFFRACTION (1.65 Å)