3SNS
Crystal structure of the C-terminal domain of Escherichia coli lipoprotein BamC
Summary for 3SNS
| Entry DOI | 10.2210/pdb3sns/pdb |
| Related | 2LAF 2YH5 |
| Descriptor | Lipoprotein 34, CHLORIDE ION (3 entities in total) |
| Functional Keywords | alpha/beta, bacterial outer membrane protein assembly, bam complex proteins, e. coli outer membrane, lipid anchored outer membrane protein, protein transport |
| Biological source | Escherichia coli |
| Cellular location | Cell outer membrane; Lipid-anchor: P0A903 |
| Total number of polymer chains | 1 |
| Total formula weight | 12927.18 |
| Authors | Kim, K.H.,Aulakh, S.,Tan, W.,Paetzel, M. (deposition date: 2011-06-29, release date: 2011-08-24, Last modification date: 2023-09-13) |
| Primary citation | Kim, K.H.,Aulakh, S.,Tan, W.,Paetzel, M. Crystallographic analysis of the C-terminal domain of the Escherichia coli lipoprotein BamC. Acta Crystallogr.,Sect.F, 67:1350-1358, 2011 Cited by PubMed 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. PubMed: 22102230DOI: 10.1107/S174430911103363X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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