4jml

Crystal structure of the TolB(P201C)-ColicinE9 TBE peptide(A33C) complex.Crystal structure of the TolB(P201C)-ColicinE9 TBE peptide(A33C) complex.

Structural highlights 4jml is a 2 chain structure with sequence from Escherichia coli dh1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: Related: 2ivz Gene: ECDH1ME8569_0700, EcDH1_2895, tolB (Escherichia coli DH1) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Porins are beta-barrel outer-membrane proteins through which small solutes and metabolites diffuse that are also exploited during cell death. We have studied how the bacteriocin colicin E9 (ColE9) assembles a cytotoxic translocon at the surface of Escherichia coli that incorporates the trimeric porin OmpF. Formation of the translocon involved ColE9's unstructured N-terminal domain threading in opposite directions through two OmpF subunits, capturing its target TolB on the other side of the membrane in a fixed orientation that triggers colicin import. Thus, an intrinsically disordered protein can tunnel through the narrow pores of an oligomeric porin to deliver an epitope signal to the cell to initiate cell death. Intrinsically disordered protein threads through the bacterial outer-membrane porin OmpF.,Housden NG, Hopper JT, Lukoyanova N, Rodriguez-Larrea D, Wojdyla JA, Klein A, Kaminska R, Bayley H, Saibil HR, Robinson CV, Kleanthous C Science. 2013 Jun 28;340(6140):1570-4. doi: 10.1126/science.1237864. PMID:23812713 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also TolB

spinqualitylabelsall models 4jml, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image