1g43
From Proteopedia
|
CRYSTAL STRUCTURE OF A FAMILY IIIA CBD FROM CLOSTRIDIUM CELLULOLYTICUM
Overview
The crystal structure of the family IIIa cellulose-binding domain (CBD), from the cellulosomal scaffoldin subunit (CipC) of Clostridium, cellulolyticum has been determined. The structure reveals a nine-stranded, jelly-roll topology which exhibits distinctive structural elements, consistent with family III CBDs that bind crystalline cellulose. These, include a well conserved calcium-binding site, a putative, cellulose-binding surface and a conserved shallow groove of unknown, function. The CipC CBD structure is very similar to the previously, elucidated family IIIa CBD from the CipA scaffoldin of C. thermocellum, with some minor differences. The CipC CBD structure was also compared with, other previously described CBD structures from families IIIc and IV, derived from the endoglucanases of Thermomonospora fusca and Cellulomonas, fimi, respectively. The possible functional consequences of structural, similarities and differences in the shallow groove and cellulose-binding, faces among various CBD families and subfamilies are discussed.
About this Structure
1G43 is a Single protein structure of sequence from Clostridium cellulolyticum with CA and ZN as ligands. Full crystallographic information is available from OCA.
Reference
Structure of a family IIIa scaffoldin CBD from the cellulosome of Clostridium cellulolyticum at 2.2 A resolution., Shimon LJ, Pages S, Belaich A, Belaich JP, Bayer EA, Lamed R, Shoham Y, Frolow F, Acta Crystallogr D Biol Crystallogr. 2000 Dec;56(Pt 12):1560-8. PMID:11092922
Page seeded by OCA on Sun Nov 25 00:49:13 2007
