2OWX
THERMUS THERMOPHILUS AMYLOMALTASE AT pH 5.6
Summary for 2OWX
| Entry DOI | 10.2210/pdb2owx/pdb |
| Related | 1ESW 1OWC 2OWW |
| Descriptor | 4-alpha-glucanotransferase, MALONATE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | beta-alpha-8 barrel, succinimide residue in main chain, transferase |
| Biological source | Thermus thermophilus |
| Total number of polymer chains | 1 |
| Total formula weight | 57722.38 |
| Authors | Barends, T.R.M.,Kaper, T.,Bultema, J.J.,Dijkhuizen, L.,van der Maarel, J.E.C.,Dijkstra, B.W. (deposition date: 2007-02-17, release date: 2007-04-03, Last modification date: 2023-11-15) |
| Primary citation | Barends, T.R.,Bultema, J.B.,Kaper, T.,van der Maarel, M.J.,Dijkhuizen, L.,Dijkstra, B.W. Three-way stabilization of the covalent intermediate in amylomaltase, an alpha-amylase-like transglycosylase. J.Biol.Chem., 282:17242-17249, 2007 Cited by PubMed Abstract: Amylomaltases are glycosyl hydrolases belonging to glycoside hydrolase family 77 that are capable of the synthesis of large cyclic glucans and the disproportionation of oligosaccharides. Using protein crystallography, we have generated a flip book movie of the amylomaltase catalytic cycle in atomic detail. The structures include a covalent glycosyl enzyme intermediate and a covalent intermediate in complex with an analogue of a co-substrate and show how the structures of both enzyme and substrate respond to the changes required by the catalytic cycle as it proceeds. Notably, the catalytic nucleophile changes conformation dramatically during the reaction. Also, Gln-256 on the 250s loop is involved in orienting the substrate in the +1 site. The absence of a suitable base in the covalent intermediate structure explains the low hydrolysis activity. PubMed: 17420245DOI: 10.1074/jbc.M701444200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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