yersiniabactin

Yersiniabactin (Ybt) is a siderophore found in the pathogenic bacteria Yersinia pestis, Yersinia pseudotuberculosis, and Yersinia enterocolitica, as well as several strains of enterobacteria including enteropathogenic Escherichia coli and Salmonella enterica. Siderophores, compounds of low molecular mass with high affinities for ferric iron, are important virulence factors in pathogenic bacteria. Iron—an essential element for life used for such cellular processes as respiration and DNA replication—is extensively chelated by host proteins like lactoferrin and ferritin; thus, the pathogen produces molecules with an even higher affinity for Fe3+ than these proteins in order to acquire sufficient iron for growth. As a part of such an iron-uptake system, yersiniabactin plays an important role in pathogenicity of Y. pestis, Y. pseudotuberculosis, and Y. entercolitica.

==Structure and coordination properties== Yersiniabactin is a four ring structure composed of carbon, hydrogen, nitrogen, oxygen, and sulfur. According to X-ray crystallography, it binds Fe3+as a 1:1 complex by three nitrogen electron pairs and three negatively charged oxygen atoms (each set in meridional positions) with a distorted octahedral structure. The Ybt-Fe3+ complex has a proton-independent formation constant of 4 x 1036.