Structure of the novel α-amylase AmyC from Thermotoga maritima

Achim Dickmanns, Meike Ballschmiter, Wolfgang Liebl, Ralf Ficner

Research output: Contribution to journalArticlepeer-review

36 Scopus citations


α-Amylases are essential enzymes in α-glucan metabolism and catalyse the hydrolysis of long sugar polymers such as amylose and starch. The crystal structure of a previously unidentified amylase (AmyC) from the hyperthermophilic organism Thermotoga maritima was determined at 2.2 Å resolution by means of MAD. AmyC lacks sequence similarity to canonical α-amylases, which belong to glycosyl hydrolase families 13, 70 and 77, but exhibits significant similarity to a group of as yet uncharacterized proteins in COG1543 and is related to glycerol hydrolase family 57 (GH-57). AmyC reveals features that are characteristic of α-amylases, such as a distorted TIM-barrel structure formed by seven β-strands and α-helices (domain A), and two additional but less well conserved domains. The latter are domain B, which contains three helices inserted in the TIM-barrel after β-sheet 2, and domain C, a five-helix region at the C-terminus. Interestingly, despite moderate sequence homology, structure comparison revealed significant similarities to a member of GH-57 with known three-dimensional structure, Thermococcus litoralis 4-glucanotransferase, and an even higher similarity to a structure of an enzyme of unknown function from Thermus thermophilus.

Original languageEnglish
Pages (from-to)262-270
Number of pages9
JournalActa Crystallographica Section D: Biological Crystallography
Issue number3
StatePublished - Mar 2006
Externally publishedYes


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