2ZK7

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

Summary for 2ZK7

• Entry DOI: 10.2210/pdb2zk7/pdb
• Related: 2DTD 2DTE 2DTX
• Descriptor: Glucose 1-dehydrogenase related protein (2 entities in total)
• Functional Keywords: rossmann fold, oxidoreductase
• Biological source: Thermoplasma acidophilum
• Total number of polymer chains: 2
• Total formula weight: 56596.79

Authors

Nishioka, T.,Yasutake, Y.,Nishiya, Y.,Tamura, N.,Tamura, T. (deposition date: 2008-03-12, release date: 2009-01-13, Last modification date: 2024-10-30)

Primary citation

Nishioka, T.,Yasutake, Y.,Nishiya, Y.,Tamura, N.,Tamura, T.
C-terminal tail derived from the neighboring subunit is critical for the activity of Thermoplasma acidophilum D-aldohexose dehydrogenase
Proteins, 74:801-807, 2009

PubMed Abstract: 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.

PubMed: 19089950
DOI: 10.1002/prot.22300

Experimental method

X-RAY DIFFRACTION (2.71 Å)