Crystal structure of the bacterial protein export chaperone secB |
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Authors: | Xu Z Knafels J D Yoshino K |
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Institution: | Department of Biological Chemistry, The University of Michigan Medical School, 1301 E. Catherine Road, Ann Arbor, Michigan 48109, USA. zhaohui@umich.edu |
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Abstract: | SecB is a bacterial molecular chaperone involved in mediating translocation of newly synthesized polypeptides across the cytoplasmic membrane of bacteria. The crystal structure of SecB from Haemophilus influenzae shows that the molecule is a tetramer organized as a dimer of dimers. Two long channels run along the side of the molecule. These are bounded by flexible loops and lined with conserved hydrophobic amino acids, which define a suitable environment for binding non-native polypeptides. The structure also reveals an acidic region on the top surface of the molecule, several residues of which have been implicated in binding to SecA, its downstream target. |
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