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Title: Starch Catabolism by a Prominent Human Gut Symbiont Is Directed by the Recognition of Amylose Helices

Abstract

The human gut microbiota performs functions that are not encoded in our Homo sapiens genome, including the processing of otherwise undigestible dietary polysaccharides. Defining the structures of proteins involved in the import and degradation of specific glycans by saccharolytic bacteria complements genomic analysis of the nutrient-processing capabilities of gut communities. Here, we describe the atomic structure of one such protein, SusD, required for starch binding and utilization by Bacteroides thetaiotaomicron, a prominent adaptive forager of glycans in the distal human gut microbiota. The binding pocket of this unique {alpha}-helical protein contains an arc of aromatic residues that complements the natural helical structure of starch and imposes this conformation on bound maltoheptaose. Furthermore, SusD binds cyclic oligosaccharides with higher affinity than linear forms. The structures of several SusD/oligosaccharide complexes reveal an inherent ligand recognition plasticity dominated by the three-dimensional conformation of the oligosaccharides rather than specific interactions with the composite sugars.

Authors:
; ; ;  [1]
  1. WU
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
USDOE
OSTI Identifier:
1006876
Resource Type:
Journal Article
Journal Name:
Structure
Additional Journal Information:
Journal Volume: 16; Journal Issue: (7) ; 07, 2008
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; AFFINITY; AROMATICS; BACTERIA; CATABOLISM; COMPLEXES; DIGESTIVE SYSTEM; FUNCTIONS; HUMAN POPULATIONS; INTERACTIONS; LIGANDS; OLIGOSACCHARIDES; PLASTICITY; POLYSACCHARIDES; PROCESSING; PROTEIN STRUCTURE; PROTEINS; RESIDUES; SACCHARIDES; STARCH

Citation Formats

Koropatkin, Nicole M, Martens, Eric C, Gordon, Jeffrey I, Smith, Thomas J, and Danforth). Starch Catabolism by a Prominent Human Gut Symbiont Is Directed by the Recognition of Amylose Helices. United States: N. p., 2009. Web. doi:10.1016/j.str.2008.03.017.
Koropatkin, Nicole M, Martens, Eric C, Gordon, Jeffrey I, Smith, Thomas J, & Danforth). Starch Catabolism by a Prominent Human Gut Symbiont Is Directed by the Recognition of Amylose Helices. United States. doi:10.1016/j.str.2008.03.017.
Koropatkin, Nicole M, Martens, Eric C, Gordon, Jeffrey I, Smith, Thomas J, and Danforth). Mon . "Starch Catabolism by a Prominent Human Gut Symbiont Is Directed by the Recognition of Amylose Helices". United States. doi:10.1016/j.str.2008.03.017.
@article{osti_1006876,
title = {Starch Catabolism by a Prominent Human Gut Symbiont Is Directed by the Recognition of Amylose Helices},
author = {Koropatkin, Nicole M and Martens, Eric C and Gordon, Jeffrey I and Smith, Thomas J and Danforth)},
abstractNote = {The human gut microbiota performs functions that are not encoded in our Homo sapiens genome, including the processing of otherwise undigestible dietary polysaccharides. Defining the structures of proteins involved in the import and degradation of specific glycans by saccharolytic bacteria complements genomic analysis of the nutrient-processing capabilities of gut communities. Here, we describe the atomic structure of one such protein, SusD, required for starch binding and utilization by Bacteroides thetaiotaomicron, a prominent adaptive forager of glycans in the distal human gut microbiota. The binding pocket of this unique {alpha}-helical protein contains an arc of aromatic residues that complements the natural helical structure of starch and imposes this conformation on bound maltoheptaose. Furthermore, SusD binds cyclic oligosaccharides with higher affinity than linear forms. The structures of several SusD/oligosaccharide complexes reveal an inherent ligand recognition plasticity dominated by the three-dimensional conformation of the oligosaccharides rather than specific interactions with the composite sugars.},
doi = {10.1016/j.str.2008.03.017},
journal = {Structure},
number = (7) ; 07, 2008,
volume = 16,
place = {United States},
year = {2009},
month = {1}
}