Structure of CBM3b of the major cellulosomal scaffoldin subunit ScaA from Acetivibrio cellulolyticus

Oren Yaniv, Yehuda Halfon, Linda J.W. Shimon, Edward A. Bayer, Raphael Lamed, Felix Frolow*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


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 languageEnglish
Pages (from-to)8-13
Number of pages6
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number1
StatePublished - 1 Jan 2012


  • Acetivibrio cellulolyticus
  • CBM3b
  • ScaA
  • cellulose-binding module
  • cellulosome
  • major scaffoldin subunit


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