1QD6

OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI

1QD6 の概要

• エントリーDOI: 10.2210/pdb1qd6/pdb
• 関連するPDBエントリー: 1QD5
• 分子名称: OUTER MEMBRANE PHOSPHOLIPASE (OMPLA), PROTEIN (OUTER MEMBRANE PHOSPHOLIPASE (OMPLA)), CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: anti-parallel beta barrel dimer, membrane protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell outer membrane ; Multi-pass membrane protein : P0A921 P0A921
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 58925.64

構造登録者

Snijder, H.J.,Ubarretxena-Belandia, I.,Blaauw, M.,Kalk, K.H.,Verheij, H.M.,Egmond, M.R.,Dekker, N.,Dijkstra, B.W. (登録日: 1999-07-09, 公開日: 1999-10-25, 最終更新日: 2024-10-09)

主引用文献

Snijder, H.J.,Ubarretxena-Belandia, I.,Blaauw, M.,Kalk, K.H.,Verheij, H.M.,Egmond, M.R.,Dekker, N.,Dijkstra, B.W.
Structural evidence for dimerization-regulated activation of an integral membrane phospholipase.
Nature, 401:717-721, 1999

PubMed Abstract: Dimerization is a biological regulatory mechanism employed by both soluble and membrane proteins. However, there are few structural data on the factors that govern dimerization of membrane proteins. Outer membrane phospholipase A (OMPLA) is an integral membrane enzyme which participates in secretion of colicins in Escherichia coli. In Campilobacter and Helicobacter pylori strains, OMPLA is implied in virulence. Its activity is regulated by reversible dimerization. Here we report X-ray structures of monomeric and dimeric OMPLA from E. coli. Dimer interactions occur almost exclusively in the apolar membrane-embedded parts, with two hydrogen bonds within the hydrophobic membrane area being key interactions. Dimerization results in functional oxyanion holes and substrate-binding pockets, which are absent in monomeric OMPLA. These results provide a detailed view of activation by dimerization of a membrane protein.

PubMed: 10537112
DOI: 10.1038/44890

実験手法

X-RAY DIFFRACTION (2.1 Å)