3K8K
Crystal structure of SusG
Summary for 3K8K
| Entry DOI | 10.2210/pdb3k8k/pdb |
| Related | 3K8L 3K8M |
| Descriptor | Alpha-amylase, susG, MAGNESIUM ION, CALCIUM ION, ... (7 entities in total) |
| Functional Keywords | amylase, alpha8/beta8 barrel, cbm, beta-sandwich, membrane protein |
| Biological source | Bacteroides thetaiotaomicron |
| Cellular location | Cell outer membrane ; Lipid-anchor : Q8A1G3 |
| Total number of polymer chains | 2 |
| Total formula weight | 152992.44 |
| Authors | Koropatkin, N.M.,Smith, T.J. (deposition date: 2009-10-14, release date: 2010-03-02, Last modification date: 2024-11-27) |
| Primary citation | Koropatkin, N.M.,Smith, T.J. SusG: A Unique Cell-Membrane-Associated alpha-Amylase from a Prominent Human Gut Symbiont Targets Complex Starch Molecules. Structure, 18:200-215, 2010 Cited by PubMed 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. PubMed: 20159465DOI: 10.1016/j.str.2009.12.010 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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