4fay

Crystal structure of a trimeric bacterial microcompartment shell protein PduB with glycerol metabolites

spinqualitylabelsall models 4fay, resolution 1.56Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4fay is a 3 chain structure with sequence from Limosilactobacillus reuteri subsp. reuteri. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.56Å Ligands: ACT, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PDUB_LIMRD One of the major shell proteins of the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation (By similarity). Probably involved in a propanediol fermentation/reuterin formation pathway (Probable).[UniProtKB:P37449] Publication Abstract from PubMed Lactobacillus reuteri metabolizes two similar three-carbon molecules, 1,2-propanediol and glycerol, within closed polyhedral subcellular bacterial organelles called bacterial microcompartments (metabolosomes). The outer shell of the propanediol-utilization (Pdu) metabolosome is composed of hundreds of mainly hexagonal protein complexes made from six types of protein subunits that share similar domain structures. The structure of the bacterial microcompartment protein PduB has a tandem structural repeat within the subunit and assembles into a trimer with pseudo-hexagonal symmetry. This trimeric structure forms sheets in the crystal lattice and is able to fit within a polymeric sheet of the major shell component PduA to assemble a facet of the polyhedron. There are three pores within the trimer and these are formed between the tandem repeats within the subunits. The structure shows that each of these pores contains three glycerol molecules that interact with conserved residues, strongly suggesting that these subunit pores channel glycerol substrate into the metabolosome. In addition to the observation of glycerol occupying the subunit channels, the presence of glycerol on the molecular threefold symmetry axis suggests a role in locking closed the central region. Substrate channels revealed in the trimeric Lactobacillus reuteri bacterial microcompartment shell protein PduB.,Pang A, Liang M, Prentice MB, Pickersgill RW Acta Crystallogr D Biol Crystallogr. 2012 Dec;68(Pt 12):1642-52. doi:, 10.1107/S0907444912039315. Epub 2012 Nov 9. PMID:23151629 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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