z-logo
open-access-imgOpen Access
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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here