1OLA

THE STRUCTURAL BASIS OF MULTISPECIFICITY IN THE OLIGOPEPTIDE-BINDING PROTEIN OPPA

1OLA の概要

• エントリーDOI: 10.2210/pdb1ola/pdb
• 分子名称: OLIGO-PEPTIDE BINDING PROTEIN, PEPTIDE VAL-LYS-PRO-GLY, URANYL (VI) ION, ... (4 entities in total)
• 機能のキーワード: binding protein
• 由来する生物種: Salmonella typhimurium
• 細胞内の位置: Periplasm: P06202
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 59819.53

構造登録者

Tame, J.,Wilkinson, A.J. (登録日: 1994-04-26, 公開日: 1994-07-31, 最終更新日: 2024-10-30)

主引用文献

Tame, J.R.,Murshudov, G.N.,Dodson, E.J.,Neil, T.K.,Dodson, G.G.,Higgins, C.F.,Wilkinson, A.J.
The structural basis of sequence-independent peptide binding by OppA protein.
Science, 264:1578-1581, 1994

PubMed Abstract: Specific protein-ligand interactions are critical for cellular function, and most proteins select their partners with sharp discrimination. However, the oligopeptide-binding protein of Salmonella typhimurium (OppA) binds peptides of two to five amino acid residues without regard to sequence. The crystal structure of OppA reveals a three-domain organization, unlike other periplasmic binding proteins. In OppA-peptide complexes, the ligands are completely enclosed in the protein interior, a mode of binding that normally imposes tight specificity. The protein fulfills the hydrogen bonding and electrostatic potential of the ligand main chain and accommodates the peptide side chains in voluminous hydrated cavities.

PubMed: 8202710

実験手法

X-RAY DIFFRACTION (2.1 Å)