Structural highlights
Function
[C9QPR1_ECOD1] Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane (By similarity).[HAMAP-Rule:MF_00923]
Publication Abstract from PubMed
In Escherichia coli, the BAM complex is essential for the assembly and insertion of outer membrane proteins (OMPs). The BAM complex is comprised of an integral beta-barrel outer membrane protein BamA and four accessory lipoproteins BamB, BamC, BamD and BamE. Here, the crystal structure of BamB is reported. The crystal of BamB diffracted to 2.0 A with one monomer in the asymmetric unit and the structure is composed of eight-bladed beta-propeller motifs. Pull-down and Western blotting assays indicate that BamB interacts directly with the POTRA 1-3 domain of BamA and the C-terminal region of the POTRA 1-3 domain plays an important role in the interaction, while the POTRA 1-2 domain is not required for the interaction.
Structure of Escherichia coli BamB and its interaction with POTRA domains of BamA.,Dong C, Yang X, Hou HF, Shen YQ, Dong YH Acta Crystallogr D Biol Crystallogr. 2012 Sep;68(Pt 9):1134-9. Epub 2012 Aug 18. PMID:22948914[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dong C, Yang X, Hou HF, Shen YQ, Dong YH. Structure of Escherichia coli BamB and its interaction with POTRA domains of BamA. Acta Crystallogr D Biol Crystallogr. 2012 Sep;68(Pt 9):1134-9. Epub 2012 Aug 18. PMID:22948914 doi:http://dx.doi.org/10.1107/S0907444912023141
