3CGI
Crystal structure of the PduU shell protein from the Pdu microcompartment
Summary for 3CGI
Entry DOI | 10.2210/pdb3cgi/pdb |
Related | 2A10 2A1B 2EWH |
Descriptor | Propanediol utilization protein pduU (2 entities in total) |
Functional Keywords | circular permutation, beta barrel, bacterial microcompartment, propanediol, signaling protein, unknown function |
Biological source | Salmonella typhimurium |
Total number of polymer chains | 4 |
Total formula weight | 54238.38 |
Authors | Crowley, C.S.,Sawaya, M.R.,Yeates, T.O. (deposition date: 2008-03-05, release date: 2008-09-02, Last modification date: 2023-08-30) |
Primary citation | Crowley, C.S.,Sawaya, M.R.,Bobik, T.A.,Yeates, T.O. Structure of the PduU Shell Protein from the Pdu Microcompartment of Salmonella Structure, 16:1324-1332, 2008 Cited by PubMed Abstract: The Pdu microcompartment is a proteinaceous, subcellular structure that serves as an organelle for the metabolism of 1,2-propanediol in Salmonella enterica. It encapsulates several related enzymes within a shell composed of a few thousand protein subunits. Recent structural studies on the carboxysome, a related microcompartment involved in CO(2) fixation, have concluded that the major shell proteins from that microcompartment form hexamers that pack into layers comprising the facets of the shell. Here we report the crystal structure of PduU, a protein from the Pdu microcompartment, representing the first structure of a shell protein from a noncarboxysome microcompartment. Though PduU is a hexamer like other characterized shell proteins, it has undergone a circular permutation leading to dramatic differences in the hexamer pore. In view of the hypothesis that microcompartment metabolites diffuse across the outer shell through these pores, the unique structure of PduU suggests the possibility of a special functional role. PubMed: 18786396DOI: 10.1016/j.str.2008.05.013 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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