This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3zqw is a 1 chain structure with sequence from Acetivibrio cellulolyticus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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 A and even at a wavelength of 0.97625 A 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.
Structure of CBM3b of the major cellulosomal scaffoldin subunit ScaA from Acetivibrio cellulolyticus.,Yaniv O, Halfon Y, Shimon LJ, Bayer EA, Lamed R, Frolow F Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jan 1;68(Pt 1):8-13. Epub , 2011 Dec 24. PMID:22232162[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Yaniv O, Halfon Y, Shimon LJ, Bayer EA, Lamed R, Frolow F. Structure of CBM3b of the major cellulosomal scaffoldin subunit ScaA from Acetivibrio cellulolyticus. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jan 1;68(Pt 1):8-13. Epub , 2011 Dec 24. PMID:22232162 doi:10.1107/S174430911104807X