4rbu
PduA K26A S40Q mutant, from Salmonella enterica serovar Typhimurium LT2PduA K26A S40Q mutant, from Salmonella enterica serovar Typhimurium LT2
Structural highlights
FunctionPublication Abstract from PubMedBacterial microcompartments are widespread prokaryotic organelles that have important and diverse roles ranging from carbon fixation to enteric pathogenesis. Current models for microcompartment function propose that their outer protein shell is selectively permeable to small molecules, but whether a protein shell can mediate selective permeability and how this occurs are unresolved questions. Here, biochemical and physiological studies of structure-guided mutants are used to show that the hexameric PduA shell protein of the 1,2-propanediol utilization (Pdu) microcompartment forms a selectively permeable pore tailored for the influx of 1,2-propanediol (the substrate of the Pdu microcompartment) while restricting the efflux of propionaldehyde, a toxic intermediate of 1,2-propanediol catabolism. Crystal structures of various PduA mutants provide a foundation for interpreting the observed biochemical and phenotypic data in terms of molecular diffusion across the shell. Overall, these studies provide a basis for understanding a class of selectively permeable channels formed by nonmembrane proteins. Selective molecular transport through the protein shell of a bacterial microcompartment organelle.,Chowdhury C, Chun S, Pang A, Sawaya MR, Sinha S, Yeates TO, Bobik TA Proc Natl Acad Sci U S A. 2015 Feb 23. pii: 201423672. PMID:25713376[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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