4c4v

Structure of the outer membrane protein insertase BamA with one POTRA domain.

spinqualitylabelsall models 4c4v, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4c4v is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [BAMA_ECOLI] Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Publication Abstract from PubMed Outer membrane protein (OMP) biogenesis is an essential process for maintaining the bacterial cell envelope and involves the beta-barrel assembly machinery (BAM) for OMP recognition, folding and assembly. In Escherichia coli this function is orchestrated by five proteins: the integral outer membrane protein BamA of the Omp85 superfamily and four associated lipoproteins. To unravel the mechanism underlying OMP folding and insertion, the structure of the E. coli BamA beta-barrel and P5 domain was determined at 3 A resolution. These data add information beyond that provided in the recently published crystal structures of BamA from Haemophilus ducreyi and Neisseria gonorrhoeae and are a valuable basis for the interpretation of pertinent functional studies. In an `open' conformation, E. coli BamA displays a significant degree of flexibility between P5 and the barrel domain, which is indicative of a multi-state function in substrate transfer. E. coli BamA is characterized by a discontinuous beta-barrel with impaired beta1-beta16 strand interactions denoted by only two connecting hydrogen bonds and a disordered C-terminus. The 16-stranded barrel surrounds a large cavity which implies a function in OMP substrate binding and partial folding. These findings strongly support a mechanism of OMP biogenesis in which substrates are partially folded inside the barrel cavity and are subsequently released laterally into the lipid bilayer. Structure of BamA, an essential factor in outer membrane protein biogenesis.,Albrecht R, Schutz M, Oberhettinger P, Faulstich M, Bermejo I, Rudel T, Diederichs K, Zeth K Acta Crystallogr D Biol Crystallogr. 2014 Jun;70(Pt 6):1779-89. doi:, 10.1107/S1399004714007482. Epub 2014 May 30. PMID:24914988 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Bam complex Insertase

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