Journal article
Molecular basis for the selectivity and specificity of ligand recognition by the family 16 carbohydrate-binding modules from Thermoanaerobacterium polysaccharolyticum ManA
The Journal of biological chemistry, Vol.283(18), pp.12415-12425
05/02/2008
DOI: 10.1074/jbc.M706513200
PMID: 18025086
Abstract
Enzymes that hydrolyze complex polysaccharides into simple sugars are modular in architecture and consist of single or multiple catalytic domains fused to targeting modules called carbohydratebinding modules (CBMs). CBMs bind to their ligands with high affinity and increase the efficiency of the catalytic components by targeting the enzymes to its substrate. Here we utilized a multidisciplinary approach to characterize each of the two family 16 carbohydrate-binding domain components of the highly active mannanase from the thermophile Thermoanaerobacterium polysaccharolyticum. These represent the first crystal structures of family 16 CBMs. Calorimetric analysis showed that although these CBMs demonstrate high specificity toward beta-1,4-linked sugars, they can engage both cello- and manno-polysaccharides. To elucidate the molecular basis for this specificity and selectivity, we have determined high resolution crystal structures of each of the two CBMs, as well as of binary complexes of CBM16-1 bound to either mannopentaose or cellopentaose. These results provide detailed molecular insights into ligand recognition and yield a framework for rational engineering experiments designed to expand the natural repertoire of these targeting modules.
Details
- Title: Subtitle
- Molecular basis for the selectivity and specificity of ligand recognition by the family 16 carbohydrate-binding modules from Thermoanaerobacterium polysaccharolyticum ManA
- Creators
- Brian Bae - University of Illinois Urbana-ChampaignSamuel Ohene-Adjei - University of Illinois Urbana-ChampaignSvetlana Kocherginskaya - University of Illinois Urbana-ChampaignRoderick I. Mackie - University of Illinois Urbana-ChampaignM. Ashley Spies - University of Illinois Urbana-ChampaignIsaac K. O. Cann - University of Illinois Urbana-ChampaignSatish K. Nair - University of Illinois Urbana-Champaign
- Resource Type
- Journal article
- Publication Details
- The Journal of biological chemistry, Vol.283(18), pp.12415-12425
- DOI
- 10.1074/jbc.M706513200
- PMID
- 18025086
- NLM abbreviation
- J Biol Chem
- ISSN
- 0021-9258
- eISSN
- 1083-351X
- Publisher
- Elsevier
- Number of pages
- 11
- Language
- English
- Date published
- 05/02/2008
- Academic Unit
- Pharmaceutical Sciences and Experimental Therapeutics; Biochemistry and Molecular Biology; Medicinal and Natural Products Chemistry
- Record Identifier
- 9984293072902771
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