PMID:22102230
| Citation |
Kim, KH, Aulakh, S, Tan, W and Paetzel, M (2011) Crystallographic analysis of the C-terminal domain of the Escherichia coli lipoprotein BamC. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67:1350-8 |
|---|---|
| Abstract |
In Gram-negative bacteria, the BAM complex catalyzes the essential process of assembling outer membrane proteins. The BAM complex in Escherichia coli consists of five proteins: one β-barrel membrane protein, BamA, and four lipoproteins, BamB, BamC, BamD and BamE. Here, the crystal structure of the C-terminal domain of E. coli BamC (BamC(C): Ala224-Ser343) refined to 1.5 Å resolution in space group H3 is reported. BamC(C) consists of a six-stranded antiparallel β-sheet, three α-helices and one 3(10)-helix. Sequence and surface analysis reveals that most of the conserved residues within BamC(C) are localized to form a continuous negatively charged groove that is involved in a major crystalline lattice contact in which a helix from a neighbouring BamC(C) binds against this surface. This interaction is topologically and architecturally similar to those seen in the substrate-binding grooves of other proteins with BamC-like folds. Taken together, these results suggest that an identified surface on the C-terminal domain of BamC may serve as an important protein-binding surface for interaction with other BAM-complex components or substrates. |
| Links |
PubMed PMC3212449 Online version:10.1107/S174430911103363X |
| Keywords |
Amino Acid Sequence; Crystallography, X-Ray; Escherichia coli/chemistry; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/isolation & purification; Lipid-Linked Proteins/chemistry; Lipid-Linked Proteins/isolation & purification; Models, Molecular; Molecular Sequence Data; Protein Folding; Protein Structure, Tertiary; Sequence Alignment; Structural Homology, Protein; Surface Properties |
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