NDLI: R161, K452 and R460 residues are vital for metal–citrate complex transport in Cit<sub>Sc</sub> from Streptomyces coelicolor

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R161, K452 and R460 residues are vital for metal–citrate complex transport in Cit_Sc from Streptomyces coelicolor

Content Provider	Royal Society of Chemistry (RSC)
Author	Li, Qi Wen Estlinbaum, Maggie Doyle, Robert P. Lensbouer, Joshua J.
Copyright Year	2010
Abstract	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.
Starting Page	342
Ending Page	347
Page Count	6
File Format	HTM / HTML PDF
ISSN	17565901
Volume Number	2
Issue Number	5
Journal	Metallomics
DOI	10.1039/b920689b
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Symporter Streptomyces Gram-positive bacteria Proton Bacteria
Content Type	Text
Resource Type	Article
Subject	Chemistry Medicine Metals and Alloys Biochemistry Biomaterials Biophysics

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