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      Structural basis for the interaction of BamB with the POTRA3–4 domains of BamA

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          Abstract

          In Escherichia coli, the Omp85 protein BamA and four lipoproteins (BamBCDE) constitute the BAM complex, which is essential for the assembly and insertion of outer membrane proteins into the outer membrane. Here, the crystal structure of BamB in complex with the POTRA3–4 domains of BamA is reported at 2.1 Å resolution. Based on this structure, the POTRA3 domain is associated with BamB viahydrogen-bonding and hydrophobic interactions. Structural and biochemical analysis revealed that the conserved residues Arg77, Glu127, Glu150, Ser167, Leu192, Leu194 and Arg195 of BamB play an essential role in interaction with the POTRA3 domain.

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          Type V protein secretion pathway: the autotransporter story.

          Ian Henderson, Fernando Navarro-García, Mickaël Desvaux … (2004)
          Gram-negative bacteria possess an outer membrane layer which constrains uptake and secretion of solutes and polypeptides. To overcome this barrier, bacteria have developed several systems for protein secretion. The type V secretion pathway encompasses the autotransporter proteins, the two-partner secretion system, and the recently described type Vc or AT-2 family of proteins. Since its discovery in the late 1980s, this family of secreted proteins has expanded continuously, due largely to the advent of the genomic age, to become the largest group of secreted proteins in gram-negative bacteria. Several of these proteins play essential roles in the pathogenesis of bacterial infections and have been characterized in detail, demonstrating a diverse array of function including the ability to condense host cell actin and to modulate apoptosis. However, most of the autotransporter proteins remain to be characterized. In light of new discoveries and controversies in this research field, this review considers the autotransporter secretion process in the context of the more general field of bacterial protein translocation and exoprotein function.
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            Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli.

            Tao Wu, Juliana Malinverni, Natividad Ruiz … (2005)
            Gram-negative bacteria have an outer membrane (OM) that functions as a barrier to protect the cell from toxic compounds such as antibiotics and detergents. The OM is a highly asymmetric bilayer composed of phospholipids, glycolipids, and proteins. Assembly of this essential organelle occurs outside the cytoplasm in an environment that lacks obvious energy sources such as ATP, and the mechanisms involved are poorly understood. We describe the identification of a multiprotein complex required for the assembly of proteins in the OM of Escherichia coli. We also demonstrate genetic interactions between genes encoding components of this protein assembly complex and imp, which encodes a protein involved in the assembly of lipopolysaccharides (LPS) in the OM. These genetic interactions suggest a role for YfgL, one of the lipoprotein components of the protein assembly complex, in a homeostatic control mechanism that coordinates the overall OM assembly process.
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              Role of a highly conserved bacterial protein in outer membrane protein assembly.

              Romé Voulhoux, Martine Bos, Jeroen Geurtsen … (2003)
              After transport across the cytoplasmic membrane, bacterial outer membrane proteins are assembled into the outer membrane. Meningococcal Omp85 is a highly conserved protein in Gram-negative bacteria, and its homolog Toc75 is a component of the chloroplast protein-import machinery. Omp85 appeared to be essential for viability, and unassembled forms of various outer membrane proteins accumulated upon Omp85 depletion. Immunofluorescence microscopy revealed decreased surface exposure of outer membrane proteins, which was particularly apparent at the cell-division planes. Thus, Omp85 is likely to play a role in outer membrane protein assembly.
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                Author and article information

                Journal
                Journal ID (publisher-id): ACSDAD
                Title: Acta Crystallographica Section D Structural Biology
                Abbreviated Title: Acta Crystallogr D Struct Biol
                Publisher: International Union of Crystallography (IUCr)
                ISSN (Print): 2059-7983
                Publication date Created: February 2016
                Publication date (Print): January 22 2016
                Volume: 72
                Issue: 2
                Pages: 236-244
                Article
                DOI: 10.1107/S2059798315024729
                SO-VID: a70a5f7e-6174-4cec-bca2-898990510c74
                Copyright © © 2016
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                http://journals.iucr.org/services/copyrightpolicy.html

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