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Structure of a C-terminal deletion mutant of Thermoplasma acidophilum aldohexose dehydrogenase (AldT)Structure of a C-terminal deletion mutant of Thermoplasma acidophilum aldohexose dehydrogenase (AldT)
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe D-aldohexose dehydrogenase from the thermoacidophilic archaeon Thermoplasma acidophilum (AldT) is a homotetrameric enzyme that catalyzes the oxidation of several D-aldohexoses, especially D-mannose. AldT comprises a unique C-terminal tail motif (residues 247-255) that shuts the active-site pocket of the neighboring subunit. The functional role of the C-terminal tail of AldT has been investigated using mutational and crystallographic analyses. A total of four C-terminal deletion mutants (Delta254, Delta253, Delta252, and Delta249) and two site-specific mutants (Y86G and P254G) were expressed by Escherichia coli and purified. Enzymatic characterization of these mutants revealed that the C-terminal tail is a requisite and that the interaction between Tyr86 and Pro254 is critical for enzyme activity. The crystal structure of the Delta249 mutant was also determined. The structure showed that the active-site loops undergo a significant conformational change, which leads to the structural deformation of the substrate-binding pocket. Proteins 2009. (c) 2008 Wiley-Liss, Inc. C-terminal tail derived from the neighboring subunit is critical for the activity of Thermoplasma acidophilumD-aldohexose dehydrogenase.,Nishioka T, Yasutake Y, Nishiya Y, Tamura N, Tamura T Proteins. 2008 Oct 21. PMID:19089950[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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