3TEF: Crystal Structure Of The Periplasmic Catecholate-Siderophore Binding Protein Vctp From Vibrio Cholerae

VctP, one of the two essential siderophore-binding PBPs from the pathogen Vibrio cholerae, plays an important role in the transport of enterobactin and vibriobactin, which have quite different configurations of iron coordination, from the periplasm to the inner membrane. The current study reports the crystal structure of VctP from V. cholerae N16961 at 1.7A resolution. A structural comparison of VctP with its homologues and the results of molecular docking indicate that enterobactin and vibriobactin share the same binding pocket. Significantly, a basic triad consisting of Arg137, Arg226 and Arg270 is used to balance the three negative charges of ferric-enterobactin, while a basic dyad consisting of Arg137 and Arg270 is used to balance the two negative charges of ferric-vibriobactin.
PDB ID: 3TEFDownload
MMDB ID: 101938
PDB Deposition Date: 2011/8/13
Updated in MMDB: 2012/08
Experimental Method:
x-ray diffraction
Resolution: 1.7  Å
Source Organism:
Similar Structures:
Biological Unit for 3TEF: monomeric; determined by author and by software (PISA)
Molecular Components in 3TEF
Label Count Molecule
Protein (1 molecule)
Iron(iii) ABC Transporter, Periplasmic Iron-compo Binding Protein
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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