3TEF

Crystal Structure of the Periplasmic Catecholate-Siderophore Binding Protein VctP from Vibrio Cholerae

Summary for 3TEF

• Entry DOI: 10.2210/pdb3tef/pdb
• Descriptor: Iron(III) ABC transporter, periplasmic iron-compound-binding protein (2 entities in total)
• Functional Keywords: siderophore-binding protein, transport protein
• Biological source: Vibrio cholerae
• Total number of polymer chains: 1
• Total formula weight: 32638.67

Authors

Liu, X.,Wang, Z.,Liu, S.,Li, N.,Chen, Y.,Zhu, C.,Zhu, D.,Wei, T.,Huang, Y.,Xu, S.,Gu, L. (deposition date: 2011-08-13, release date: 2012-08-15, Last modification date: 2024-03-20)

Primary citation

Liu, X.,Du, Q.,Wang, Z.,Liu, S.,Li, N.,Chen, Y.,Zhu, C.,Zhu, D.,Wei, T.,Huang, Y.,Xu, S.,Gu, L.
Crystal structure of periplasmic catecholate-siderophore binding protein VctP from Vibrio cholerae at 1.7 A resolution
Febs Lett., 586:1240-1244, 2012

PubMed Abstract: 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 1.7Å 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.

PubMed: 22575663
DOI: 10.1016/j.febslet.2012.03.043

Experimental method

X-RAY DIFFRACTION (1.698 Å)