Starch catabolism by a prominent human gut symbiont is directed by the recognition of amylose helices.
Starch catabolism by a prominent human gut symbiont is directed by the recognition of amylose helices.
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DOI:
10.1016/j.str.2008.03.017
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发表时间:
2008-07
期刊:
影响因子:
--
通讯作者:
Smith TJ
中科院分区:
文献类型:
--
作者:
Koropatkin NM;Martens EC;Gordon JI;Smith TJ
The human gut microbiota performs functions that are not encoded in our H. sapiens genome including the processing of otherwise undigestible dietary polysaccharides. Defining the structures of proteins involved in 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 α-helical protein contains an arc of aromatic residues that complements the natural helical structure of starch and imposes this conformation on bound maltoheptaose. Further, 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.
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影响因子:
3.4
作者:
Cho, JC;Giovannoni, SJ
通讯作者:
Giovannoni, SJ
影响因子:
5.1
作者:
Bauer, Margarete;Kube, Michael;Gloeckner, Frank Oliver
通讯作者:
Gloeckner, Frank Oliver
影响因子:
5.6
作者:
IMBERTY, A;CHANZY, H;TRAN, V
通讯作者:
TRAN, V
DOI:
10.1107/s0907444998003254
发表时间:
1998-09-01
期刊:
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
影响因子:
--
作者:
Brunger, AT;Adams, PD;Warren, GL
通讯作者:
Warren, GL
DOI:
10.1016/0019-2791(72)90096-1
发表时间:
1972-01-01
期刊:
IMMUNOCHEMISTRY
影响因子:
--
作者:
HORNICK, CL;KARUSH, F
通讯作者:
KARUSH, F