4UA8
EUR_01830 (maltotriose-binding protein) complexed with maltotriose
Summary for 4UA8
| Entry DOI | 10.2210/pdb4ua8/pdb |
| Related | 4UAC |
| Related PRD ID | PRD_900009 |
| Descriptor | Carbohydrate ABC transporter substrate-binding protein, CUT1 family (TC 3.A.1.1.-), alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, 1,2-ETHANEDIOL, ... (5 entities in total) |
| Functional Keywords | solute-binding protein maltotriose abc, transport protein |
| Biological source | Eubacterium rectale DSM 17629 |
| Total number of polymer chains | 1 |
| Total formula weight | 43355.55 |
| Authors | Koropatkin, N.M.,Orlovsky, N.I. (deposition date: 2014-08-08, release date: 2014-12-03, Last modification date: 2023-12-27) |
| Primary citation | Cockburn, D.W.,Orlovsky, N.I.,Foley, M.H.,Kwiatkowski, K.J.,Bahr, C.M.,Maynard, M.,Demeler, B.,Koropatkin, N.M. Molecular details of a starch utilization pathway in the human gut symbiont Eubacterium rectale. Mol.Microbiol., 95:209-230, 2015 Cited by PubMed Abstract: Eubacterium rectale is a prominent human gut symbiont yet little is known about the molecular strategies this bacterium has developed to acquire nutrients within the competitive gut ecosystem. Starch is one of the most abundant glycans in the human diet, and E. rectale increases in vivo when the host consumes a diet rich in resistant starch, although it is not a primary degrader of this glycan. Here we present the results of a quantitative proteomics study in which we identify two glycoside hydrolase 13 family enzymes, and three ABC transporter solute-binding proteins that are abundant during growth on starch and, we hypothesize, work together at the cell surface to degrade starch and capture the released maltooligosaccharides. EUR_21100 is a multidomain cell wall anchored amylase that preferentially targets starch polysaccharides, liberating maltotetraose, whereas the membrane-associated maltogenic amylase EUR_01860 breaks down maltooligosaccharides longer than maltotriose. The three solute-binding proteins display a range of glycan-binding specificities that ensure the capture of glucose through maltoheptaose and some α1,6-branched glycans. Taken together, we describe a pathway for starch utilization by E. rectale DSM 17629 that may be conserved among other starch-degrading Clostridium cluster XIVa organisms in the human gut. PubMed: 25388295DOI: 10.1111/mmi.12859 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.54 Å) |
Structure validation
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