The basal and major pilins in the Corynebacterium diphtheriae SpaA pilus adopt similar structures that competitively react with the pilin polymerase.

Autor: Sue CK; Department of Chemistry and Biochemistry, University of California, Los Angeles, California, USA.; UCLA-DOE Institute for Genomics and Proteomics, University of California, Los Angeles, California, USA., Cheung NA; UCLA-DOE Institute for Genomics and Proteomics, University of California, Los Angeles, California, USA.; Molecular Biology Institute, University of California, Los Angeles, California, USA., Mahoney BJ; Department of Chemistry and Biochemistry, University of California, Los Angeles, California, USA.; UCLA-DOE Institute for Genomics and Proteomics, University of California, Los Angeles, California, USA., McConnell SA; Department of Chemistry and Biochemistry, University of California, Los Angeles, California, USA.; UCLA-DOE Institute for Genomics and Proteomics, University of California, Los Angeles, California, USA., Scully JM; Department of Chemistry and Biochemistry, University of California, Los Angeles, California, USA.; UCLA-DOE Institute for Genomics and Proteomics, University of California, Los Angeles, California, USA., Fu JY; Department of Chemistry and Biochemistry, University of California, Los Angeles, California, USA.; UCLA-DOE Institute for Genomics and Proteomics, University of California, Los Angeles, California, USA., Chang C; Molecular Biology Institute, University of California, Los Angeles, California, USA.; Division of Oral and Systemic Health Sciences, School of Dentistry, University of California, Los Angeles, California, USA., Ton-That H; Molecular Biology Institute, University of California, Los Angeles, California, USA.; Division of Oral and Systemic Health Sciences, School of Dentistry, University of California, Los Angeles, California, USA., Loo JA; Department of Chemistry and Biochemistry, University of California, Los Angeles, California, USA.; UCLA-DOE Institute for Genomics and Proteomics, University of California, Los Angeles, California, USA.; Molecular Biology Institute, University of California, Los Angeles, California, USA., Clubb RT; Department of Chemistry and Biochemistry, University of California, Los Angeles, California, USA.; UCLA-DOE Institute for Genomics and Proteomics, University of California, Los Angeles, California, USA.; Molecular Biology Institute, University of California, Los Angeles, California, USA.
Jazyk: angličtina
Zdroj: Biopolymers [Biopolymers] 2024 Jan; Vol. 115 (1), pp. e23539. Date of Electronic Publication: 2023 May 25.
DOI: 10.1002/bip.23539
Abstrakt: Many species of pathogenic gram-positive bacteria display covalently crosslinked protein polymers (called pili or fimbriae) that mediate microbial adhesion to host tissues. These structures are assembled by pilus-specific sortase enzymes that join the pilin components together via lysine-isopeptide bonds. The archetypal SpaA pilus from Corynebacterium diphtheriae is built by the Cd SrtA pilus-specific sortase, which crosslinks lysine residues within the SpaA and SpaB pilins to build the shaft and base of the pilus, respectively. Here, we show that Cd SrtA crosslinks SpaB to SpaA via a K139(SpaB)-T494(SpaA) lysine-isopeptide bond. Despite sharing only limited sequence homology, an NMR structure of SpaB reveals striking similarities with the N-terminal domain of SpaA ( N SpaA) that is also crosslinked by Cd SrtA. In particular, both pilins contain similarly positioned reactive lysine residues and adjacent disordered AB loops that are predicted to be involved in the recently proposed "latch" mechanism of isopeptide bond formation. Competition experiments using an inactive SpaB variant and additional NMR studies suggest that SpaB terminates SpaA polymerization by outcompeting N SpaA for access to a shared thioester enzyme-substrate reaction intermediate.
(© 2023 Wiley Periodicals LLC.)
Databáze: MEDLINE
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