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Crystal structure of SpaE basal pilin from Lactobacillus rhamnosus GG - Orthorhombic formCrystal structure of SpaE basal pilin from Lactobacillus rhamnosus GG - Orthorhombic form
Structural highlights
FunctionPublication Abstract from PubMedFor some Gram-positive genera and species, the long-extended and adhesive sortase-dependent pilus plays an essential role during host colonization, biofilm formation, and immune modulation. Lactobacillus rhamnosus GG is a gut-adapted commensal strain that harbors the operonic genes for the SpaCBA and SpaFED pili, both being comprised of three different protein subunits termed the backbone, tip, and basal pilins. Crystal structures of the backbone pilins (SpaA and SpaD) have recently been solved, and here we describe the high-resolution (1.5A) structural determination of the SpaE basal pilin. SpaE consists of two immunoglobulin-like CnaB domains, with each displaying a spontaneously formed internal isopeptide bond, though apparently slow forming in the N-terminal domain. Remarkably, SpaE contains an atypically lengthy unstructured C-terminal tail, along with an YPKN pilin motif peptide, which is normally reserved for backbone subunits. Based on our analysis of the crystal structure data, we provide a molecular model for the basal positioning of the SpaE pilin within the SpaFED pilus. Crystal structure of basal pilin SpaE reveals the molecular basis of its incorporation in the lactobacillar SpaFED pilus.,Megta AK, Mishra AK, Palva A, von Ossowski I, Krishnan V J Struct Biol. 2019 Jul 1;207(1):74-84. doi: 10.1016/j.jsb.2019.04.016. Epub 2019, Apr 23. PMID:31026587[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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