PMID:21937441
| Citation |
Kim, KH, Aulakh, S and Paetzel, M (2011) Crystal structure of β-barrel assembly machinery BamCD protein complex. J. Biol. Chem. 286:39116-21 |
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| Abstract |
The β-barrel assembly machinery (BAM) complex of Escherichia coli is a multiprotein machine that catalyzes the essential process of assembling outer membrane proteins. The BAM complex consists of five proteins: one membrane protein, BamA, and four lipoproteins, BamB, BamC, BamD, and BamE. Here, we report the first crystal structure of a Bam lipoprotein complex: the essential lipoprotein BamD in complex with the N-terminal half of BamC (BamC(UN) (Asp(28)-Ala(217)), a 73-residue-long unstructured region followed by the N-terminal domain). The BamCD complex is stabilized predominantly by various hydrogen bonds and salt bridges formed between BamD and the N-terminal unstructured region of BamC. Sequence and molecular surface analyses revealed that many of the conserved residues in both proteins are found at the BamC-BamD interface. A series of truncation mutagenesis and analytical gel filtration chromatography experiments confirmed that the unstructured region of BamC is essential for stabilizing the BamCD complex structure. The unstructured N terminus of BamC interacts with the proposed substrate-binding pocket of BamD, suggesting that this region of BamC may play a regulatory role in outer membrane protein biogenesis. |
| Links |
PubMed PMC3234736 Online version:10.1074/jbc.M111.298166 |
| Keywords |
Bacterial Outer Membrane Proteins/chemistry; Bacterial Outer Membrane Proteins/genetics; Bacterial Outer Membrane Proteins/metabolism; Crystallography, X-Ray; Escherichia coli K12/chemistry; Escherichia coli K12/genetics; Escherichia coli K12/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Lipid-Linked Proteins/chemistry; Lipid-Linked Proteins/genetics; Lipid-Linked Proteins/metabolism; Protein Stability; Protein Structure, Quaternary; Protein Structure, Tertiary |
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