
Structure of CBM3b of the major cellulosomal scaffoldin subunit ScaA from Acetivibrio cellulolyticus
Author(s) -
Yaniv Oren,
Halfon Yehuda,
Shimon Linda J. W.,
Bayer Edward A.,
Lamed Raphael,
Frolow Felix
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911104807x
Subject(s) - protein subunit , microbiology and biotechnology , chemistry , biology , biochemistry , gene
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.