Maltose-binding protein

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== Structural highlights ==
== Structural highlights ==
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The <scene name='47/471830/Cv/4'>MBP sugar binding cleft is rich with protein-ligand hydrogen bonds</scene><ref>PMID:9309217</ref>. Water molecules shown as red spheres.
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The <scene name='47/471830/Cv/5'>MBP sugar binding cleft is rich with protein-ligand hydrogen bonds</scene><ref>PMID:9309217</ref>. Water molecules are shown as red spheres.
</StructureSection>
</StructureSection>
==3D structures of maltose-binding protein==
==3D structures of maltose-binding protein==

Revision as of 10:06, 9 July 2019

E. coli maltose-binding protein complex with maltose (PDB entry 1anf)

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3D structures of maltose-binding protein

Updated on 09-July-2019

References

  1. Kapust RB, Waugh DS. Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci. 1999 Aug;8(8):1668-74. PMID:10452611 doi:http://dx.doi.org/10.1110/ps.8.8.1668
  2. Sun P, Tropea JE, Waugh DS. Enhancing the solubility of recombinant proteins in Escherichia coli by using hexahistidine-tagged maltose-binding protein as a fusion partner. Methods Mol Biol. 2011;705:259-74. doi: 10.1007/978-1-61737-967-3_16. PMID:21125392 doi:http://dx.doi.org/10.1007/978-1-61737-967-3_16
  3. Quiocho FA, Spurlino JC, Rodseth LE. Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor. Structure. 1997 Aug 15;5(8):997-1015. PMID:9309217

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