5D6V

PduJ K25A mutant, from Salmonella enterica serovar Typhimurium LT2, PduJ mutant

Summary for 5D6V

• Entry DOI: 10.2210/pdb5d6v/pdb
• Descriptor: Carboxysome shell protein (2 entities in total)
• Functional Keywords: bacterial microcompartment shell protein, structural protein
• Biological source: Salmonella typhimurium
• Total number of polymer chains: 1
• Total formula weight: 9848.27

Authors

Chun, S.,Sawaya, M.R.,Yeates, T.O. (deposition date: 2015-08-13, release date: 2016-06-29, Last modification date: 2024-03-06)

Primary citation

Chowdhury, C.,Chun, S.,Sawaya, M.R.,Yeates, T.O.,Bobik, T.A.
The function of the PduJ microcompartment shell protein is determined by the genomic position of its encoding gene.
Mol.Microbiol., 101:770-783, 2016

PubMed Abstract: Bacterial microcompartments (MCPs) are complex organelles that consist of metabolic enzymes encapsulated within a protein shell. In this study, we investigate the function of the PduJ MCP shell protein. PduJ is 80% identical in amino acid sequence to PduA and both are major shell proteins of the 1,2-propanediol (1,2-PD) utilization (Pdu) MCP of Salmonella. Prior studies showed that PduA mediates the transport of 1,2-PD (the substrate) into the Pdu MCP. Surprisingly, however, results presented here establish that PduJ has no role 1,2-PD transport. The crystal structure revealed that PduJ was nearly identical to that of PduA and, hence, offered no explanation for their differential functions. Interestingly, however, when a pduJ gene was placed at the pduA chromosomal locus, the PduJ protein acquired a new function, the ability to mediate 1,2-PD transport into the Pdu MCP. To our knowledge, these are the first studies to show that that gene location can determine the function of a MCP shell protein. We propose that gene location dictates protein-protein interactions essential to the function of the MCP shell.

PubMed: 27561553
DOI: 10.1111/mmi.13423

Experimental method

X-RAY DIFFRACTION (1.5 Å)