3ZQW

Structure of CBM3b of major scaffoldin subunit ScaA from Acetivibrio cellulolyticus

Summary for 3ZQW

• Entry DOI: 10.2210/pdb3zqw/pdb
• Related: 3ZU8 3ZUC
• Descriptor: CELLULOSOMAL SCAFFOLDIN, CALCIUM ION, 1,2-ETHANEDIOL, ... (6 entities in total)
• Functional Keywords: carbohydrate-binding protein, cellulosome
• Biological source: ACETIVIBRIO CELLULOLYTICUS
• Total number of polymer chains: 1
• Total formula weight: 17187.36

Authors

Yaniv, O.,Halfon, Y.,Lamed, R.,Frolow, F. (deposition date: 2011-06-12, release date: 2012-01-11, Last modification date: 2024-05-08)

Primary citation

Yaniv, O.,Halfon, Y.,Shimon, L.J.W.,Bayer, E.A.,Lamed, R.,Frolow, F.
Structure of Cbm3B of the Major Scaffoldin Subunit Scaa from Acetivibrio Cellulolyticus
Acta Crystallogr.,Sect.F, 68:8-, 2012

PubMed 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.

PubMed: 22232162
DOI: 10.1107/S174430911104807X

Experimental method

X-RAY DIFFRACTION (1.07 Å)