R161, K452 and R460 residues are vital for metal-citrate complex transport in CitSc from streptomyces coelicolor

Joshua J. Lensbouer, Qi Wen Li, Maggie Estlinbaum, Robert P. Doyle

Research output: Contribution to journalArticlepeer-review

4 Scopus citations


Recent discoveries have been made that demonstrate Gram-positive bacteria can transport metal-citrate complexes through the CitMHS family of proteins in symport with H+ ions. The CitMHS family of transporters investigated to date have the ability to selectively transport only certain metal-citrate complexes. Despite sharing amino acid sequence similarity as high as 73%; predicting what complexes are transported remains difficult. The iron-citrate transporter from Streptomyces coelicolor has been mutated at three postulated critical sites (R161, K452 and R460) based on activity modeling against the LacY permease. All three mutants eliminate or greatly reduce uptake of metal-citrate complexes tested. The implications of this are discussed.

Original languageEnglish (US)
Pages (from-to)342-347
Number of pages6
Issue number5
StatePublished - May 27 2010

ASJC Scopus subject areas

  • Chemistry (miscellaneous)
  • Biophysics
  • Biomaterials
  • Biochemistry
  • Metals and Alloys


Dive into the research topics of 'R161, K452 and R460 residues are vital for metal-citrate complex transport in Cit<sub>Sc</sub> from streptomyces coelicolor'. Together they form a unique fingerprint.

Cite this