4RBU
PduA K26A S40Q mutant, from Salmonella enterica serovar Typhimurium LT2
Summary for 4RBU
| Entry DOI | 10.2210/pdb4rbu/pdb |
| Related | 4RBT 4RBV |
| Descriptor | Propanediol utilization protein PduA, SULFATE ION (3 entities in total) |
| Functional Keywords | bacterial micrcompartment shell protein, structural protein |
| Biological source | Salmonella enterica serovar Typhimurium |
| Total number of polymer chains | 9 |
| Total formula weight | 94224.20 |
| Authors | Chun, S.,Sawaya, M.R.,Yeates, T.O. (deposition date: 2014-09-13, release date: 2015-02-18, Last modification date: 2023-09-20) |
| Primary citation | Chowdhury, 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: 25713376DOI: 10.1073/pnas.1423672112 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.79 Å) |
Structure validation
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