Journal
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
Volume 70, Issue -, Pages 522-534Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S139900471302926X
Keywords
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Funding
- Israel Science Foundation (ISF) [715/12, 500/10, 1349/13]
- Sidney E. Frank Foundation through the Israel Science Foundation [24/11]
- US-Israel Binational Science Foundation (BSF)
- Israeli Center of Research Excellence (I-CORE Center) Program of the Planning and Budgeting Committee [152/11]
- Ministry of Environmental Protection
- Grand Technion Energy Program, comprising part of The Leona M. and Harry B. Helmsley Charitable Trust
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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.
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