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.
Original language | English |
---|---|
Pages (from-to) | 8-13 |
Number of pages | 6 |
Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
Volume | 68 |
Issue number | 1 |
DOIs | |
State | Published - 1 Jan 2012 |
Keywords
- Acetivibrio cellulolyticus
- CBM3b
- ScaA
- cellulose-binding module
- cellulosome
- major scaffoldin subunit