2J4M

Double dockerin from Piromyces equi Cel45A

2J4M の概要

• エントリーDOI: 10.2210/pdb2j4m/pdb
• 関連するPDBエントリー: 1E8P 1E8Q 2J4N
• NMR情報: BMRB: 7285
• 分子名称: ENDOGLUCANASE 45A (1 entity in total)
• 機能のキーワード: dockerin, cellulosome, protein binding, small cysteine-rich
• 由来する生物種: PIROMYCES EQUI
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10910.52

構造登録者

Nagy, T.,Tunnicliffe, R.B.,Higgins, L.D.,Walters, C.,Gilbert, H.J.,Williamson, M.P. (登録日: 2006-09-01, 公開日: 2007-09-25, 最終更新日: 2024-11-20)

主引用文献

Nagy, T.,Tunnicliffe, R.B.,Higgins, L.D.,Walters, C.,Gilbert, H.J.,Williamson, M.P.
Characterization of a Double Dockerin from the Cellulosome of the Anaerobic Fungus Piromyces Equi.
J.Mol.Biol., 373:612-, 2007

PubMed Abstract: The assembly into supramolecular complexes of proteins having complementary activities is central to cellular function. One such complex of considerable biological and industrial significance is the plant cell wall-degrading apparatus of anaerobic microorganisms, termed the cellulosome. A central feature of bacterial cellulosomes is a large non-catalytic protein, the scaffoldin, which contains multiple cohesin domains. An array of digestive enzymes is incorporated into the cellulosome through the interaction of the dockerin domains, present in the catalytic subunits, with the cohesin domains that are present in the scaffoldin. By contrast, in anaerobic fungi, such as Piromyces equi, the dockerins of cellulosomal enzymes are often present in tandem copies; however, the identity of the cognate cohesin domains in these organisms is unclear, hindering further biotechnological development of the fungal cellulosome. Here, we characterise the solution structure and function of a double-dockerin construct from the P. equi endoglucanase Cel45A. We show that the two domains are connected by a flexible linker that is short enough to keep the binding sites of the two domains on adjacent surfaces, and allows the double-dockerin construct to bind more tightly to cellulosomes than a single domain and with greater coverage. The double dockerin binds to the GH3 beta-glucosidase component of the fungal cellulosome, which is thereby identified as a potential scaffoldin.

PubMed: 17869267
DOI: 10.1016/J.JMB.2007.08.007

実験手法

SOLUTION NMR