3ZU8

STRUCTURE OF CBM3B OF MAJOR SCAFFOLDIN SUBUNIT SCAA FROM ACETIVIBRIO CELLULOLYTICUS DETERMINED ON THE NIKEL ABSORPTION EDGE

3ZU8 の概要

• エントリーDOI: 10.2210/pdb3zu8/pdb
• 関連するPDBエントリー: 3ZQW 3ZUC
• 分子名称: CELLULOSOMAL SCAFFOLDIN, CALCIUM ION, 1,2-ETHANEDIOL, ... (6 entities in total)
• 機能のキーワード: sugar binding protein, cellulosome
• 由来する生物種: ACETIVIBRIO CELLULOLYTICUS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17187.36

構造登録者

Yaniv, O.,Halfon, Y.,Lamed, R.,Frolow, F. (登録日: 2011-07-17, 公開日: 2012-01-11, 最終更新日: 2024-05-08)

主引用文献

Yaniv, O.,Halfon, Y.,Shimon, L.J.W.,Bayer, E.A.,Lamed, R.,Frolow, F.
Structure of Cbm3B of the Major Scaffoldin Subunit Scaa from Acetivibrio Cellulolyticus
Acta Crystallogr.,Sect.F, 68:8-, 2012

PubMed Abstract: The carbohydrate-binding module (CBM) of the major scaffoldin subunit ScaA of the cellulosome of Acetivibrio cellulolyticus is classified as a family 3b CBM and binds strongly to cellulose. The CBM3b was overexpressed, purified and crystallized, and its three-dimensional structure was determined. The structure contained a nickel-binding site located at the N-terminal region in addition to a 'classical' CBM3b calcium-binding site. The structure was also determined independently by the SAD method using data collected at the Ni-absorption wavelength of 1.48395 Å and even at a wavelength of 0.97625 Å in a favourable case. The new scaffoldin-borne CBM3 structure reported here provides clear evidence for the proposition that a family 3b CBM may be accommodated in scaffoldin subunits and functions as the major substrate-binding entity of the cellulosome assembly.

PubMed: 22232162
DOI: 10.1107/S174430911104807X

実験手法

X-RAY DIFFRACTION (1.801 Å)