3MY2
Crystal structure of LptC
Summary for 3MY2
| Entry DOI | 10.2210/pdb3my2/pdb |
| Descriptor | Lipopolysaccharide export system protein lptC (2 entities in total) |
| Functional Keywords | lptc, lipopolysaccharide export pathway, structural genomics, scottish structural proteomics facility, sspf, transport protein |
| Biological source | Escherichia coli |
| Cellular location | Cell inner membrane; Single-pass membrane protein: P0ADV9 |
| Total number of polymer chains | 1 |
| Total formula weight | 20241.98 |
| Authors | Tran, A.X.,Dong, C.,Whitfield, C.,Scottish Structural Proteomics Facility (SSPF) (deposition date: 2010-05-09, release date: 2010-09-01, Last modification date: 2024-10-09) |
| Primary citation | Tran, A.X.,Dong, C.,Whitfield, C. Structure and functional analysis of LptC, a conserved membrane protein involved in the lipopolysaccharide export pathway in Escherichia coli. J.Biol.Chem., 285:33529-33539, 2010 Cited by PubMed Abstract: LptC is a conserved bitopic inner membrane protein from Escherichia coli involved in the export of lipopolysaccharide from its site of synthesis in the cytoplasmic membrane to the outer membrane. LptC forms a complex with the ATP-binding cassette transporter, LptBFG, which is thought to facilitate the extraction of lipopolysaccharide from the inner membrane and release it into a translocation pathway that includes the putative periplasmic chaperone LptA. Cysteine modification experiments established that the catalytic domain of LptC is oriented toward the periplasm. The structure of the periplasmic domain is described at a resolution of 2.2-Å from x-ray crystallographic data. The periplasmic domain of LptC consists of a twisted boat structure with two β-sheets in apposition to each other. The β-sheets contain seven and eight antiparallel β-strands, respectively. This structure bears a high degree of resemblance to the crystal structure of LptA. Like LptA, LptC binds lipopolysaccharide in vitro. In vitro, LptA can displace lipopolysaccharide from LptC (but not vice versa), consistent with their locations and their proposed placement in a unidirectional export pathway. PubMed: 20720015DOI: 10.1074/jbc.M110.144709 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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