3ZUC
Structure of CBM3b of major scaffoldin subunit ScaA from Acetivibrio cellulolyticus determined from the crystals grown in the presence of Nickel
Summary for 3ZUC
| Entry DOI | 10.2210/pdb3zuc/pdb |
| Related | 3ZQW 3ZU8 |
| Descriptor | CELLULOSOMAL SCAFFOLDIN, CALCIUM ION, 1,2-ETHANEDIOL, ... (6 entities in total) |
| Functional Keywords | crystalline cellulose-binding protein, sugar 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: 2011-07-18, release date: 2012-01-11, Last modification date: 2023-12-20) |
| 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 Cited by 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: 22232162DOI: 10.1107/S174430911104807X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.001 Å) |
Structure validation
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