2MPR

MALTOPORIN FROM SALMONELLA TYPHIMURIUM

2MPR の概要

• エントリーDOI: 10.2210/pdb2mpr/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900065
• 分子名称: MALTOPORIN, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-beta-D-glucopyranose, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: outer membrane protein, oligosaccharide binding, sugar transport, phage recognition
• 由来する生物種: Salmonella typhimurium
• 細胞内の位置: Cell outer membrane; Multi-pass membrane protein: P26466
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 145747.00

構造登録者

Meyer, J.E.W.,Schulz, G.E. (登録日: 1997-02-07, 公開日: 1997-04-01, 最終更新日: 2024-10-23)

主引用文献

Meyer, J.E.,Hofnung, M.,Schulz, G.E.
Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside.
J.Mol.Biol., 266:761-775, 1997

PubMed Abstract: The maltodextrin-specific (malto-)porin from Salmonella typhimurium has been crystallized. Its three-dimensional structure was determined at 2.4 A resolution (1 A = 0.1 nm). A comparison with the structure of the homologous porin from Escherichia coli as well as with the sequences of other related porins showed that there are regions of appreciable sequence and structure variability, despite close overall similarity. The maltoporin structure was analyzed with a bound nitrophenyl-maltotrioside as well as without ligand. Maltotrioside binding had a negligible effect on the polypeptide structure. It binds at the pore eyelet assuming a conformation close to the natural amylose helix.

PubMed: 9102468
DOI: 10.1006/jmbi.1996.0823

実験手法

X-RAY DIFFRACTION (2.4 Å)