SusG: a unique cell-membrane-associated alpha-amylase from a prominent human gut symbiont targets complex starch molecules

Structure. 2010 Feb 10;18(2):200-15. doi: 10.1016/j.str.2009.12.010.

Abstract

SusG is an alpha-amylase and part of a large protein complex on the outer surface of the bacterial cell and plays a major role in carbohydrate acquisition by the animal gut microbiota. Presented here, the atomic structure of SusG has an unusual extended, bilobed structure composed of amylase at one end and an unprecedented internal carbohydrate-binding motif at the other. Structural studies further demonstrate that the carbohydrate-binding motif binds maltooligosaccharide distal to, and on the opposite side of, the amylase catalytic site. SusG has an additional starch-binding site on the amylase domain immediately adjacent to the active cleft. Mutagenesis analysis demonstrates that these two additional starch-binding sites appear to play a role in catabolism of insoluble starch. However, elimination of these sites has only a limited effect, suggesting that they may have a more important role in product exchange with other Sus components.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acarbose / metabolism
  • Amino Acid Sequence
  • Bacterial Outer Membrane Proteins / chemistry*
  • Bacterial Outer Membrane Proteins / genetics
  • Bacterial Outer Membrane Proteins / metabolism*
  • Bacteroides / enzymology*
  • Bacteroides / genetics
  • Binding Sites
  • Carbohydrate Conformation
  • Carbohydrate Sequence
  • Cell Membrane / enzymology
  • Crystallography, X-Ray
  • Enzyme Inhibitors / metabolism
  • Gastrointestinal Tract / metabolism
  • Gastrointestinal Tract / microbiology*
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Oligosaccharides / chemistry
  • Oligosaccharides / metabolism
  • Protein Binding
  • Protein Structure, Tertiary
  • Starch / chemistry
  • Starch / metabolism*
  • Symbiosis
  • alpha-Amylases / chemistry*
  • alpha-Amylases / genetics
  • alpha-Amylases / metabolism*

Substances

  • Bacterial Outer Membrane Proteins
  • Enzyme Inhibitors
  • Oligosaccharides
  • maltooligosaccharides
  • Starch
  • alpha-Amylases
  • Acarbose