Part:BBa_K2812000
Carbohydrate-binding domain from MpIBP
Carbohydrate binding domain from the Marinomonas primoryensis ice-binding protein (MpIBP). It requires millimolar concentrations of calcium ions to properly fold into a globular β-fold. A coordinated calcium ion is used to bind sugar moieties, such as glucose. Unfolding of the domain can be induced by the addition of EDTA, which chelates the calcium ions and prevents binding of sugar moieties. It does not require the presence of other domains to fold and therefore it can be used as a modular protein domain to bind sugar moieties. TU Eindhoven 2018 used the carbohydrate binding domain from MpIBP to tether E. coli bacteria to dextran, a glucose-based polymer.
Usage and Biology
The Marinomonas primoryensis ice-binding protein is a 1.5-MDa adhesin used by the Antarctic bacterium M. primoryensis to bind to ice and diatoms to position itself on top of the water column to access nutrients and oxygen. The carbohydrate binding domain from this protein is used to bind extracellular polysaccharides to form microcolonies and to tether M. primoryensis to other photosynthetic microorganisms.
Carbohydrate Binding Assay
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
//collections/biofilm
//proteindomain
//proteindomain/affinity
//proteindomain/binding
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