4b9c | pdb_00004b9c

Biomass sensoring modules from putative Rsgi-like proteins of Clostridium thermocellum resemble family 3 carbohydrate-binding module of cellulosome

spinqualitylabelsall models 4b9c, resolution 1.17Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4b9c is a 1 chain structure with sequence from Cloth. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The anaerobic, thermophilic, cellulosome-producing bacterium Clostridium thermocellum relies on a variety of carbohydrate-active enzymes in order to efficiently break down complex carbohydrates into utilizable simple sugars. The regulation mechanism of the cellulosomal genes was unknown until recently, when genomic analysis revealed a set of putative operons in C. thermocellum that encode sigma(I) factors (i.e. alternative sigma factors that control specialized regulon activation) and their cognate anti-sigma(I) factor (RsgI). These putative anti-sigma(I)-factor proteins have modules that are believed to be carbohydrate sensors. Three of these modules were crystallized and their three-dimensional structures were solved. The structures show a high overall degree of sequence and structural similarity to the cellulosomal family 3 carbohydrate-binding modules (CBM3s). The structures of the three carbohydrate sensors (RsgI-CBM3s) and a reference CBM3 are compared in the context of the structural determinants for the specificity of cellulose and complex carbohydrate binding. Fine structural variations among the RsgI-CBM3s appear to result in alternative substrate preferences for each of the sensors. Fine-structural variance of family 3 carbohydrate-binding modules as extracellular biomass-sensing components of Clostridium thermocellum anti-sigma(I) factors.,Yaniv O, Fichman G, Borovok I, Shoham Y, Bayer EA, Lamed R, Shimon LJ, Frolow F Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):522-34. doi:, 10.1107/S139900471302926X. Epub 2014 Jan 31. PMID:24531486 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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