Bam complex: Difference between revisions
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<StructureSection load=' | <StructureSection load='' size='340' side='right' caption='E. coli BamA barrel domain (PDB code [[4n75]])' scene='70/706705/Cv/2'> | ||
== Function == | == Function == | ||
The '''Bam''' (β-Barrel Assembly Machinery) drives the assembly of β-barrel proteins into the outer membrane of gram-negative bacteria. | The '''Bam''' (β-Barrel Assembly Machinery) drives the assembly of β-barrel proteins into the outer membrane of gram-negative bacteria.<ref>PMID:19182809</ref> | ||
== Structural highlights == | == Structural highlights == | ||
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*'''BamA''' contains five structurally homologous POTRA (POlypeptide TRAnslocation associated) domains. The POTRA domain has a β-α-α-β-β conformation. BamA barrel and at least a subset of its POTRAs are essential for viability. BamA was found also in mitochondria and chloroplasts.<br /> | *'''BamA''' contains five structurally homologous POTRA (POlypeptide TRAnslocation associated) domains. The POTRA domain has a β-α-α-β-β conformation. BamA barrel and at least a subset of its POTRAs are essential for viability. BamA was found also in mitochondria and chloroplasts.<br /> | ||
*'''BamD''' is composed of multiple tetratricopeptide (TPR) repeats packed into a superhelical structure. TPR is a motif containing 2 antiparallel α-helices. TPRs are found in scaffold multiprotein complexes and are involved in protein-protein interactions. | *'''BamD''' is composed of multiple tetratricopeptide (TPR) repeats packed into a superhelical structure. TPR is a motif containing 2 antiparallel α-helices. TPRs are found in scaffold multiprotein complexes and are involved in protein-protein interactions. | ||
== 3D Structures of Bam complex == | == 3D Structures of Bam complex == | ||
[[Bam complex 3D structures]] | |||
</StructureSection> | |||
== References == | == References == | ||
<references/> | <references/> | ||
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