Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 68, Issue -, Pages 8-13Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S174430911104807X
Keywords
CBM3b; cellulose-binding module; major scaffoldin subunit; ScaA; cellulosome</; kwd>; Acetivibrio cellulolyticus
Funding
- Israel Science Foundation (ISF) [293/08]
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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 angstrom and even at a wavelength of 0.97625 angstrom 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.
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