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4QIF

Crystal Structure of PduA with edge mutation K26A and pore mutation S40H

Summary for 4QIF
Entry DOI10.2210/pdb4qif/pdb
Related3NGK 4P2S 4PPD
DescriptorPropanediol utilization protein PduA, S-1,2-PROPANEDIOL, SULFATE ION, ... (7 entities in total)
Functional Keywordsbmc domain, structural protein, potassium, glycerol, 1-2 propanediol, tartaric acid, sulfate ion
Biological sourceSalmonella enterica subsp. enterica serovar Typhimurium
Total number of polymer chains9
Total formula weight97960.66
Authors
Pang, A.H.,Sawaya, M.R.,Yeates, T.O. (deposition date: 2014-05-30, release date: 2015-02-18, Last modification date: 2024-02-28)
Primary citationChowdhury, C.,Chun, S.,Pang, A.,Sawaya, M.R.,Sinha, S.,Yeates, T.O.,Bobik, T.A.
Selective molecular transport through the protein shell of a bacterial microcompartment organelle.
Proc.Natl.Acad.Sci.USA, 112:2990-2995, 2015
Cited by
PubMed Abstract: Bacterial 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.
PubMed: 25713376
DOI: 10.1073/pnas.1423672112
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9951 Å)
Structure validation

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