4FAY

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

Summary for 4FAY

• Entry DOI: 10.2210/pdb4fay/pdb
• Descriptor: Microcompartments protein, GLYCEROL, ACETATE ION, ... (4 entities in total)
• Functional Keywords: bmc domain, shell protein, glycerol-binding protein
• Biological source: Lactobacillus reuteri
• Total number of polymer chains: 3
• Total formula weight: 82779.63

Authors

Pang, A.H.,Prentice, M.B.,Pickersgill, R.W. (deposition date: 2012-05-22, release date: 2012-11-21, Last modification date: 2024-04-03)

Primary citation

Pang, A.,Liang, M.,Prentice, M.B.,Pickersgill, R.W.
Substrate channels revealed in the trimeric Lactobacillus reuteri bacterial microcompartment shell protein PduB.
Acta Crystallogr.,Sect.D, 68:1642-1652, 2012

PubMed Abstract: 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.

PubMed: 23151629
DOI: 10.1107/S0907444912039315

Experimental method

X-RAY DIFFRACTION (1.56 Å)