2zk7

Structure of a C-terminal deletion mutant of Thermoplasma acidophilum aldohexose dehydrogenase (AldT)

spinqualitylabelsall models 2zk7, resolution 2.71Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2zk7 is a 2 chain structure with sequence from Thermoplasma acidophilum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.71Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9HK51_THEAC Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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