@article{3d4de112398147d5908a4429aca777d8,
title = "Fine-structural variance of family 3 carbohydrate-binding modules as extracellular biomass-sensing components of Clostridium thermocellum anti-σI factors",
abstract = "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 σI factors (i.e. alternative σ factors that control specialized regulon activation) and their cognate anti- σI factor (RsgI). These putative anti-σI- 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.",
keywords = "Clostridium thermocellum, RsgI-CBM3, anti-σ factors, family 3 carbohydrate-binding modules",
author = "Oren Yaniv and Galit Fichman and Ilya Borovok and Yuval Shoham and Bayer, {Edward A.} and Raphael Lamed and Shimon, {Linda J.W.} and Felix Frolow",
year = "2014",
month = feb,
doi = "10.1107/S139900471302926X",
language = "אנגלית",
volume = "70",
pages = "522--534",
journal = "Acta Crystallographica Section D: Biological Crystallography",
issn = "0907-4449",
publisher = "John Wiley & Sons Inc.",
number = "2",
}