1FX3
CRYSTAL STRUCTURE OF H. INFLUENZAE SECB
Summary for 1FX3
| Entry DOI | 10.2210/pdb1fx3/pdb |
| Descriptor | PROTEIN-EXPORT PROTEIN SECB (2 entities in total) |
| Functional Keywords | protein trasnport, translocation, transport protein |
| Biological source | Haemophilus influenzae |
| Total number of polymer chains | 4 |
| Total formula weight | 76585.20 |
| Authors | Xu, Z.,Knafels, J.D.,Yoshino, K. (deposition date: 2000-09-25, release date: 2000-12-06, Last modification date: 2024-02-07) |
| Primary citation | Xu, Z.,Knafels, J.D.,Yoshino, K. Crystal structure of the bacterial protein export chaperone secB. Nat.Struct.Biol., 7:1172-1177, 2000 Cited by PubMed 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. PubMed: 11101901DOI: 10.1038/82040 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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