Structural highlights
Publication Abstract from PubMed
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.
Crystal structure of periplasmic catecholate-siderophore binding protein VctP from Vibrio cholerae at 1.7 A resolution.,Liu X, Du Q, Wang Z, Liu S, Li N, Chen Y, Zhu C, Zhu D, Wei T, Huang Y, Xu S, Gu L FEBS Lett. 2012 Apr 24;586(8):1240-4. Epub 2012 Mar 28. PMID:22575663[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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. 2012 Apr 24;586(8):1240-4. Epub 2012 Mar 28. PMID:22575663 doi:10.1016/j.febslet.2012.03.043
