| Structural highlights
Function
ESPP_ECO57 Serine protease capable of cleaving pepsin A and human coagulation factor V, which may contribute to the mucosal hemorrhage observed in hemorrhagic colitis.[1] [2]
Publication Abstract from PubMed
The outer membrane structure is common in Gram-negative bacteria, mitochondria and chloroplasts, and contains outer membrane beta-barrel proteins (OMPs) that are essential interchange portals of materials(1-3). All known OMPs share the antiparallel beta-strand topology(4), implicating a common evolutionary origin and conserved folding mechanism. Models have been proposed for bacterial beta-barrel assembly machinery (BAM) to initiate OMP folding(5,6); however, mechanisms by which BAM proceeds to complete OMP assembly remain unclear. Here we report intermediate structures of BAM assembling an OMP substrate, EspP, demonstrating sequential conformational dynamics of BAM during the late stages of OMP assembly, which is further supported by molecular dynamics simulations. Mutagenic in vitro and in vivo assembly assays reveal functional residues of BamA and EspP for barrel hybridization, closure and release. Our work provides novel insights into the common mechanism of OMP assembly.
Structural basis of BAM-mediated outer membrane beta-barrel protein assembly.,Shen C, Chang S, Luo Q, Chan KC, Zhang Z, Luo B, Xie T, Lu G, Zhu X, Wei X, Dong C, Zhou R, Zhang X, Tang X, Dong H Nature. 2023 May;617(7959):185-193. doi: 10.1038/s41586-023-05988-8. Epub 2023 , Apr 26. PMID:37100902[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Brunder W, Schmidt H, Karch H. EspP, a novel extracellular serine protease of enterohaemorrhagic Escherichia coli O157:H7 cleaves human coagulation factor V. Mol Microbiol. 1997 May;24(4):767-78. PMID:9194704
- ↑ Szabady RL, Peterson JH, Skillman KM, Bernstein HD. An unusual signal peptide facilitates late steps in the biogenesis of a bacterial autotransporter. Proc Natl Acad Sci U S A. 2005 Jan 4;102(1):221-6. Epub 2004 Dec 22. PMID:15615856 doi:http://dx.doi.org/10.1073/pnas.0406055102
- ↑ Shen C, Chang S, Luo Q, Chan KC, Zhang Z, Luo B, Xie T, Lu G, Zhu X, Wei X, Dong C, Zhou R, Zhang X, Tang X, Dong H. Structural basis of BAM-mediated outer membrane β-barrel protein assembly. Nature. 2023 May;617(7959):185-193. PMID:37100902 doi:10.1038/s41586-023-05988-8
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