3Q54

Crystal structure of Escherichia coli BamB

Summary for 3Q54

• Entry DOI: 10.2210/pdb3q54/pdb
• Descriptor: Outer membrane assembly lipoprotein YfgL (2 entities in total)
• Functional Keywords: lipoprotein, bamb, lipid binding protein
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 39317.72

Authors

Dong, C.,Hou, H.,Yang, X. (deposition date: 2010-12-27, release date: 2012-05-09, Last modification date: 2024-02-21)

Primary citation

Dong, C.,Yang, X.,Hou, H.F.,Shen, Y.Q.,Dong, Y.H.
Structure of Escherichia coli BamB and its interaction with POTRA domains of BamA.
Acta Crystallogr.,Sect.D, 68:1134-1139, 2012

PubMed Abstract: 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 β-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 Å with one monomer in the asymmetric unit and the structure is composed of eight-bladed β-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.

PubMed: 22948914
DOI: 10.1107/S0907444912023141

Experimental method

X-RAY DIFFRACTION (2.004 Å)