3MPB

Z5688 from E. coli O157:H7 bound to fructose

3MPB の概要

• エントリーDOI: 10.2210/pdb3mpb/pdb
• 関連するPDBエントリー: 3KMH
• 分子名称: Sugar isomerase, MANGANESE (II) ION, ACETATE ION, ... (6 entities in total)
• 機能のキーワード: cupin, beta barrel, structural genomics, montreal-kingston bacterial structural genomics initiative, bsgi, isomerase
• 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: 56404.43

構造登録者

van Staalduinen, L.M.,Jia, Z.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (登録日: 2010-04-26, 公開日: 2010-07-21, 最終更新日: 2024-11-27)

主引用文献

van Staalduinen, L.M.,Park, C.S.,Yeom, S.J.,Adams-Cioaba, M.A.,Oh, D.K.,Jia, Z.
Structure-based annotation of a novel sugar isomerase from the pathogenic E. coli O157:H7.
J.Mol.Biol., 401:866-881, 2010

PubMed Abstract: Prokaryotes can use a variety of sugars as carbon sources in order to provide a selective survival advantage. The gene z5688 found in the pathogenic Escherichia coli O157:H7 encodes a "hypothetical" protein of unknown function. Sequence analysis identified the gene product as a putative member of the cupin superfamily of proteins, but no other functional information was known. We have determined the crystal structure of the Z5688 protein at 1.6 A resolution and identified the protein as a novel E. coli sugar isomerase (EcSI) through overall fold analysis and secondary-structure matching. Extensive substrate screening revealed that EcSI is capable of acting on d-lyxose and d-mannose. The complex structure of EcSI with fructose allowed the identification of key active-site residues, and mutagenesis confirmed their importance. The structure of EcSI also suggested a novel mechanism for substrate binding and product release in a cupin sugar isomerase. Supplementation of a nonpathogenic E. coli strain with EcSI enabled cell growth on the rare pentose d-lyxose.

PubMed: 20615418
DOI: 10.1016/j.jmb.2010.06.063

実験手法

X-RAY DIFFRACTION (1.91 Å)