2X26

Crystal structure of the periplasmic aliphatic sulphonate binding protein SsuA from Escherichia coli

2X26 の概要

• エントリーDOI: 10.2210/pdb2x26/pdb
• 分子名称: PERIPLASMIC ALIPHATIC SULPHONATES-BINDING PROTEIN, GLYCEROL (3 entities in total)
• 機能のキーワード: transport protein
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 67645.02

構造登録者

Beale, J.,Lee, S.,Iwata, S.,Beis, K. (登録日: 2010-01-11, 公開日: 2010-04-14, 最終更新日: 2023-12-20)

主引用文献

Beale, J.,Lee, S.Y.,Iwata, S.,Beis, K.
Structure of the Aliphatic Sulfonate-Binding Protein Ssua from Escherichia Coli
Acta Crystallogr.,Sect.F, 66:391-, 2010

PubMed Abstract: Sulfur is an essential component for the biosynthesis of the sulfur-containing amino acids L-methionine and L-cysteine. Under sulfur-starvation conditions, bacteria are capable of scavenging sulfur from sulfur-containing compounds and transporting it across membranes. Here, the crystal structure of the periplasmic aliphatic sulfonate-binding protein SsuA from Escherichia coli is reported at 1.75 A resolution in the substrate-free state. The overall structure of SsuA resembles the structures of other periplasmic binding proteins and contains two globular domains that form a cleft. Comparison with other periplasmic binding proteins revealed that one of the domains has been displaced by a rigid movement of 17 degrees . Interestingly, the tight crystal packing appears to be mediated by a 13-amino-acid tail from the cloning that folds within the cleft of the next monomer.

PubMed: 20383006
DOI: 10.1107/S1744309110006226

実験手法

X-RAY DIFFRACTION (1.75 Å)