7VG9

Crystal structure of phosphotransbutyrylase from Clostridium acetobutylicum

Summary for 7VG9

• Entry DOI: 10.2210/pdb7vg9/pdb
• Descriptor: Phosphate butyryltransferase, SULFATE ION (3 entities in total)
• Functional Keywords: transferase
• Biological source: Clostridium acetobutylicum
• Total number of polymer chains: 8
• Total formula weight: 280138.40

Authors

Kim, S.,Kim, K.-J. (deposition date: 2021-09-15, release date: 2021-10-27, Last modification date: 2023-11-29)

Primary citation

Kim, S.,Kim, K.J.
Crystal structure and molecular mechanism of phosphotransbutyrylase from Clostridium acetobutylicum .
J Microbiol Biotechnol., 31:1-9, 2021

PubMed Abstract: Acetone-butanol-ethanol (ABE) fermentation by the anaerobic bacterium has been considered a promising process of industrial biofuel production. Phosphotransbutyrylase (phosphate butyryltransferase, PTB) plays a crucial role in butyrate metabolism by catalyzing the reversible conversion of butyryl-CoA into butyryl phosphate. Here, we report the crystal structure of PTB from the host for ABE fermentation, , (PTB) at a 2.9 Å resolution. The overall structure of the PTB monomer is quite similar to those of other acyltransferases, with some regional structural differences. The monomeric structure of PTB consists of two distinct domains, the N- and C-terminal domains. The active site cleft was formed at the interface between the two domains. Interestingly, the crystal structure of PTB contained eight molecules per asymmetric unit, forming an octamer, and the size-exclusion chromatography experiment also suggested that the enzyme exists as an octamer in solution. The structural analysis of PTB identifies the substrate binding mode of the enzyme and comparisons with other acyltransferase structures lead us to speculate that the enzyme undergoes a conformational change upon binding of its substrate.

PubMed: 34584034
DOI: 10.4014/jmb.2109.09036

Experimental method

X-RAY DIFFRACTION (2.91 Å)